Women have traditionally heen victims of healthcare mistreatment, but how?
The Context
There is a long running trope of women not being taken seriously when they visit a doctor or clinical office and it has sparked confrontation on social media sites like Instagram and Twitter. Gender based discrimination is rampant in many professions including medical fields and it affects patients greatly. It also carries into how women of color, disability, mental condition and diverse body types are often treated unsatisfactorily and misdiagnosed.
The How
Factors facing female patients include a multitude of facets such as obesity or mental health disorders. Obesity specifically is strongly judged by many doctors since it can cause type 2 diabetes and coronary heart disease which leads some biased professionals to conclude that any problems an obese woman faces are caused by that trait. Also, if a patient is frequently showing up to doctor visits, their issues can be overlooked as just another mental health episode brought on by anxiety or even ptsd. Women are 2-3 times more likely to develop both of those disorders compared to men.
The Why
There are a lot of bias when it comes to female patients between their health professionals but why? This is likely because of personal discrimination in one part, recognized as a result of implicit personal bias. Another reason can be cultural norms that the doctor and patient are separated by, making it harder for women seeking treatment. This can be combatted if more women advocate for personal rights in professional healthcare spaces like clinics and do personal research to make sure they aren’t getting misdiagnosed.
There are nurses around the world, but how did this job come to exist?
The Beginning
During the 18th century nursing as a job began to become fully formed. This is because many wars such as the 1854 European Crimean War was occurring and help was needed across all fronts. The most influential nurse of their time, Florence Nightingale and her team helped to patch up wounded soldiers during this war. Formal training of nurses during this time period show that Florence marked the pathway for nursing as a professional career.
The Middle
In the 90s and early 2000s, nursing was starting to be taken more seriously in respect to doctors, and higher education was sought out for those pursuing nursing careers. Also more roles for nurses rather than just one were growing such as Advanced nurse practitioner, clinical nurse specialists and nursing assistants. Also, nursing research and medicine institutions were established in countries such as America.
Our Present
In modern times it is easy to see nursing as a well respected job that many people recognize to be professional. However, there are still those who hold biases about nursing because they do not understand the many roles around it. They also hold bias because of misunderstanding history and thinking nurses are traditionally only assistants to doctors. Nurses play a pivotal role in society and healthcare overall and the more education improves and technology advances, we are able to see the continuous accomplishments of nurses in our developing world today.
Women’s History Month is known as the time of year when we celebrate the achievements of and recognize the struggles women have faced throughout the years. It is usually celebrated in the United Kingdom and Australia but has been acknowledged in several other countries, including America.
History of Women’s History Month
It originated in California in 1978 as a local celebration. The Sonoma County Commission organized the first celebration as a full week Women’s History event beginning on March 8th.
There were essay contests, children giving presentations in class, and a parade to start with the celebration activities!
By the 1980s, it began to be nationally celebrated in the U.S by President Jimmy Carter.
In 1987, Congress passed the law designating March as the official Women’s History Month.
Because that was the first day of the week it was celebrated, March 8th is recognized as International Women’s Day.
Influential Women in the Medical Field
There are many Influential women in the world, but the medical field is where we want to focus on here for one of the many ways that they shine.
First, we’re going to start off with nurses since that’s our domain.
Florence Nightingale: During the Crimean War of the 1800s, this nurse revolutionized healthcare by utilizing the resources necessary to keep fighters going. She established nursing as a position that was taken seriously and respected equally.
Clara Barton: Also active in the 1800s, this healthcare pioneer founded the American Red Cross. Her work in aiding soldiers during the Civil War establishes her as one of the most influential nurses of her time.
Mary Eliza Mahoney: This nurse was the very first African American nurse to receive and complete professional training in the field. She was also an active advocate for racial equality.
Next, we’re going to focus on scientists and researchers and their amazing work as women in the medical field.
Margaret Sanger: As an active birth control activist and nurse who lived to 1966, she joined the fight for women’s reproductive rights. Her efforts led to the creation of Planned Parenthood, a reproductive health clinic.
Antonio Novello: An influential woman in history who’s still alive today, Antonio was the first Hispanic woman, and even the first woman Surgeon General of the United States, which is inspiring to women across the nation.
How to Celebrate WHM?
You can celebrate Women’s History Month in multiple ways…
Spreading a hashtag online
Volunteering with a Women’s Rights organization
Planning something special for the women in your life
Writing a letter of appreciation to your teachers, health professionals, friends or the female members of government in your local county or even nation
Learning about your rights as a woman or a supporter of women’s autonomy
American Heart Month is a time to wear red and celebrate your awareness for heart disease, the #1 leading cause of death in the United States
History of AMH
President Lyndon B Johnson established this month in 1964.
Recognizing the efforts of physicians, doctors, and the struggle of patients with heart disease and cardiovascular problems is the main cause behind this month.
How to Celebrate?
Some ways to celebrate this month are by eating healthy to avoid heart disease, exercising, spreading awareness online, and volunteering at hospitals to assist the affected patients.
Alzheimer’s disease is a common type of dementia that can result in a decline of cognitive functions such as language, attention, comprehension, memory, and judgment. It can be a hindrance in daily activities, and independence, and cannot be cured, but treatment may help. Common symptoms are short-term memory loss, impairment in judgment, language disorder, agitation, and sleep disturbances (Kumar, Sidhu, and Goyal). AD can affect lifestyle by removing the abilities of reasoning and memory. Alzheimer’s disease is grouped in amyloidosis which are disorders with an accumulation of misfolded and unfolded proteins. Often there is an accumulation of Aβ (amyloid-beta peptide) in the medial temporal lobe and neocortical structures. Alzheimer’s disease is often characterized by neuritic plaques, neurofibrillary tangles, and Aβ oligomers. Tau proteins and amyloids play a significant role in Alzheimer’s disease. It can assist in forming neuritic plaques, neurofibrillary tangles, and Aβ oligomers which can cause toxicity. Through this paper, we will explore how neuritic plaques, neurofibrillary tangles, and Aβ oligomers form. We will study the finding of a kinase protein associated with Alzheimer’s disease and the impact of Asp664.
Misfolded Proteins
When there is a neurodivergent disease, in the transition of target proteins from α-helix to a β-sheet form they obtain toxicity. Transitioning from α-helix to a β-sheet is often seen in amyloid deposits and physiological functions becoming pathological. These transitions can encourage protein aggregation and release hydrophobic amino acid residues. Toxic proteins may interact with other native proteins and transition them into a toxic state. These new toxic proteins may repeat this cycle with other native proteins resulting in more toxicity and detrimental damage. Proteins require their amino acids to be folded correctly in order to function properly, therefore, if the protein is misfolded it can form insoluble aggregates and become toxic. Without the proper clearance, misfolded proteins may accumulate resulting in Alzheimer’s disease.
In diseases, hIAPP misfoldings are found and it can be toxic when combined with human islet β-cells. Membranes can affect hIAPP misfolding in two ways, first being targeted by hIAPP oligomers to create toxicity. Second, membranes can help speed up the chemical reaction of misfolding when hIAPP and negatively charged membranes interact. A misfolding with a membrane involved happens through an α-helical intermediate and accelerates based on ionic strength. Researchers Apostolidou, Jayasinghe, and Langen used EPR spectroscopy and molecular modeling to further investigate α-helical, membrane-bound hIAPP. In their findings, residues 20-29, an amyloidogenic region of hIAPP, encourage the formation of secondary structure and cause aggregation. Due to membrane interactions, residues 21 and 22 are badly folded which is of importance because membrane interactions help form the β-sheet structure. With the additional factor of membrane interactions transforming the process of hIAPP molecule encounters into a two-dimensional process, membrane-mediated hIAPP misfolding accelerates (Apostolidou).
Risk factors
A factor that can increase this is old age because, in the process of aging, we acquire more mutations and changes in our protein structures. Changes in our protein structure increase the chances of an accumulation of misfolded proteins. An environmental factor that can increase risk is substances that may affect mitochondrial function. Damage to the mitochondrial function can result in oxidative damage to proteins. There may also be genetic factors these mutations can affect the disease differently from the different mutations and combinations of the gene.
Neuritic plaques
Alois Alzheimer, a German psychiatrist, found amyloid plaques in the brain of his first patient who was experiencing memory loss. Alzheimer’s disease is often an accumulation of abnormal neuritic plaques which have a core of extracellular amyloid beta-peptide. These beta-amyloid peptides originate from an amyloid precursor and divide from APP through the proteases alpha, beta, and gamma-secretase. Through this cleavage, it can result in aggregated fibrillar amyloid proteins which are favored by Beta-amyloid 42 (Kumar, Sidhu, and Goyal). There may also be 40 or 42 aa long Aβ peptide fragments discharged which can combine and form into insoluble Aβ clumps and oligomers. These insoluble Aβ clumps and oligomers gather around neurons and can have toxic effects. Aβ directly affects neurotoxicity and neural function which can lead to cognitive impairments if plaques accumulate in the hippocampus, amygdala, and cerebral cortex.
Structure of brains and neurons of a healthy brain in comparison with an Alzheimer’s disease brain.
^1 Breijyeh, Zeinab, and Rafik Karaman. “Comprehensive Review on Alzheimer’s Disease: Causes and Treatment.” Molecules (Basel, Switzerland) vol. 25,24 5789. 8 Dec. 2020, doi:10.3390/molecules25245789
Neurofibrillary tangles
Neurofibrillary tangles formed by the protein tau are more associated with Alzheimer’s disease. Tau proteins support microtubule assembly but can become hyperphosphorylated from aggregation of extracellular beta-amyloid. As a result, tau aggregates form settling in neurons, twisting into paired helical filaments, and creating neurofibrillary tangles (Kumar, Sidhu, and Goyal). Accumulation of tangles in neural perikaryal cytoplasm, axons, and dendrites can reduce cytoskeletal microtubules and tubulin-associated proteins. The evolution of neurofibrillary tangles can be put into three stages, the first happening before it tangles. In this stage, accumulated phosphorylated tau proteins gather in the somatodendritic compartment without paired helical filaments forming. In the next stage, mature neurofibrillary tangles possess filament aggregation and a displaced nucleus in the periphery part of the soma. Lastly, they become extracellular tangles from filamentous tau protein causing a neuronal loss (Ashraf).
Neurofilaments are microfilaments located in the soma, axon, and dendrites. They support and regulate axons making them a large part of the neuronal cytoskeleton. Neurofibrillary tangles are groups of paired helically twisted filaments that occur in pyramidal cells and neurons. These may be neurofilaments or microtubules which form from intracellular hyperphosphorylation of tau protein. The twisted fibers of tau protein damage axonal support in the range of the cell body and many synapses. The purpose of tau protein is to support microtubules by binding to them. When a tau protein is hyperphosphorylated it can no longer support microtubules because it is unable to bind to it. As the tau protein is not binded, they will clump with each other creating neurofibrillary tangles. These neurofibrillary tangles eventually damage intercellular functions and have been linked with neuropsychiatric behaviors such as aggression (Ashraf).
Aβ oligomers
The failure of Aβ peptide clearance can lead to the accumulation of Aβ in brain arteries. These aggregate states of Aβ may be in the form of oligomers which would be small and soluble oligomers that can contain 5-6 monomeric units. Aβ oligomers with a smaller diameter are more likely to fuse with synaptic clefts causing neuronal and synaptic dysfunction. Oligomerization can happen when the concentration of Aβ increases and there is a higher Aβ42/Aβ40 ratio at the beginning of amyloid plaque formation. Consequently, there may be formation of Aβ deposits which can cause inflammatory responses, synaptic spine loss, and neuritic dystrophy. One of the greatest factors in Aβ induced toxicity is Aβ structure as the β-sheet is the dominant structure of Aβ oligomers (Ashraf).
Signal transduction
APP can generate neurotoxic β-amyloid peptides and a second neurotoxic peptide through Asp664. Researchers conducted a study to identify signaling mechanisms and to understand the contribution of Asp664. Through the study of comparing animals with Alzheimer’s disease, the researchers were able to discover a kinase protein that contributes to Alzheimer’s disease that was found more in platelet-derived growth factor B-chain promoter-driven APP transgenic mice that do not have a functional Asp664 caspase cleavage site. The researchers found differences between the platelet-derived growth factor B-chain promoter-driven APP transgenic mice and the platelet-derived growth factor B-chain promoter-driven APP transgenic mice with the absence of a functional Asp664.
The experiment was conducted using antibodies, human autopsy material, transgenic mouse lines, and western blots. Through immunohistochemical and immunoblotting studies on mice with Alzheimer-like neuropathology, an increase in active p21-activated kinases was observed in platelet-derived growth factor B-chain promoter-driven APP transgenic mice. From assessing hippocampal levels it is evident that a functional Asp664 cleavage site is required to increase active p21-activated kinases. Transgenic platelet-derived growth factor B-chain promoter-driven APP transgenic mice had greater p21-activated kinases activation and neurons with active p21-activated kinases. In comparison with transgenic mice possessing a mutated Asp664, there was no significant increase in p21-activated kinase activation or neurons with active p21-activated kinases.
To determine whether the PAK changes in platelet-derived growth factor B-chain promoter-driven APP transgenic mice applied to human AD, researchers used immunohistochemical labeling on subjects that were either neuropathologically normal, early AD changes, moderate AD neuropathology, or severe AD. In the subjects, there was a decrease in p21-activated kinase immunoreactivity. Other studies have found that a signaling mechanism of AD neuropathology is a functional cleavage of APP at Asp664. The data shows that p21-activated kinases can be impacted by cleavage at Asp664 (Nguyen).
Conclusion
The purpose of this paper is to study the role of misfolded proteins in Alzheimer’s disease. Misfolded proteins play a significant part in Alzheimer’s disease and can lead to toxicity and aggregation. When target proteins transform from α-helix to a β-sheet form, toxic proteins are formed. These proteins can transition native proteins into toxic proteins which becomes an ongoing cycle. Factors that may increase the chances of misfolding are aging, damage to mitochondrial function, and genetic factors. An accumulation of neuritic plaques is often found in Alzheimer’s disease which have a core of extracellular amyloid beta-peptide that formed from an amyloid precursor. Often associated with Alzheimer’s disease are neurofibrillary tangles which form from tau protein. When tau protein is hyperphosphorylated from aggregation of extracellular beta-amyloid it can form into paired helical filaments that become neurofibrillary tangles. These neurofibrillary tangles can cause damage and neuropsychiatric behaviors. Accumulation of Aβ can form into Aβ oligomers which can result in neuronal and synaptic dysfunction. Lastly, cleavage at Asp664 can affect p21-activated kinase which contributes to Alzheimer’s disease. Despite all the research on proteins in Alzheimer’s disease, the large build-up of amyloid and tau protein is not fully understood. There are still questions as to why these large build-ups of protein happen and how to prevent it.
Works Cited
Apostolidou, Melania et al. “Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding.” The Journal of biological chemistry vol. 283,25 (2008): 17205-10. doi:10.1074/jbc.M801383200
Ashraf, Ghulam M et al. “Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus.” CNS & neurological disorders drug targets vol. 13,7 (2014): 1280-93. doi:10.2174/1871527313666140917095514
Breijyeh, Zeinab, and Rafik Karaman. “Comprehensive Review on Alzheimer’s Disease: Causes and Treatment.” Molecules (Basel, Switzerland) vol. 25,24 5789. 8 Dec. 2020, doi:10.3390/molecules25245789
DeToma, Alaina S et al. “Misfolded proteins in Alzheimer’s disease and type II diabetes.” Chemical Society reviews vol. 41,2 (2012): 608-21. doi:10.1039/c1cs15112f Gustafson, D R et al. “Adiposity indicators and dementia over 32 years in Sweden.” Neurology vol. 73,19 (2009): 1559-66. doi:10.1212/WNL.0b013e3181c0d4b6
Kumar A, Sidhu J, Goyal A, et al. Alzheimer Disease. [Updated 2022 Jun 5]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2023 Jan-. Available from: https://www.ncbi.nlm.nih.gov/books/NBK499922/
Nguyen, Thuy-Vi V et al. “Signal transduction in Alzheimer disease: p21-activated kinase signaling requires C-terminal cleavage of APP at Asp664.” Journal of neurochemistry vol. 104,4 (2008): 1065-80. doi:10.1111/j.1471-4159.2007.05031.x
Reitz, Christiane et al. “Epidemiology of Alzheimer disease.” Nature reviews. Neurology vol. 7,3 (2011): 137-52. doi:10.1038/nrneurol.2011.2
Pediatricians are medical doctors whose specific care is in the care of children. If pediatricians could be a flavor they would be vanilla. Vanilla is a very comforting, warm, and sweet flavor that describes pediatricians since they provide a heartwarming sense of nurturing and comfort to their young patients. Vanilla is a relaxing, warm hugged feeling and flavor that reminds you of sweet memories. Their gentle and reassuring care gives that balance of sweetness and comfort.
Dermatologist
Dermatologists are doctors who specifically specialize in the skin. If dermatologists could be a flavor they would be citrus, specifically lemons. Citrus fruits are very cleansing and powerful nutrients they have. Which is a dermatologist’s goal to help approach healthy, brightening, and radiant skin for their patients. Which lemons do have a brightening flavor and give a taste of clarity.
Neurologist
A neurologist is a doctor who specializes in diagnosing and treating diseases in the brain. If neurologists could be a flavor it would be a rich mocha flavor with coffee. Neurologists have a complex way of knowledge including the thoughts and layers of the brain. The rich mocha and coffee flavor give it the nature of the human brain and all these interlinked pathways that happen. The coffee shows their expertise and ability to understand the mind. It’s full of rich layers in the brain and what’s underneath everyone like the layers of coffee.
Cardiologist
A cardiologist is a specialist in the heart and blood vessels. If cardiologists could be a flavor it would be tart strawberry sorbet. Cardiologists have a sweet and tangy balance connecting their knowledge in cardiology and heart health. The tart flavor comes from being able to cut complex medical issues while caring for each and every patient which is where the sweet comes from.
Psychiatrist
A psychiatrist is a doctor who specializes and treats mental conditions. If psychiatrists could be a flavor they would be warm cinnamon. The aroma and taste of cinnamon give a sense of warmth and joy because of its feeling of calmness. These are the qualities psychiatrists have in the depth they add including warm-heartedness to their patients. They help them with life’s obstacles and give them a sense of security. Cinnamon gives a sweet-spice flavor with a comforting smell. Psychiatrists give a sense of comfort to their patients while they help and listen to what they’re saying.
Radiologists
A radiologist is a specialist in seeing and treating conditions they see in X-rays, mammograms, MRIs, and CT scans. If radiologists could be a flavor it would be dark cherry. Dark cherry has a complex and intense flavor which relates to their medical X-rays and the complex imagining they interpret. Cherries have seeds in them which you discover which is like how Radiologists discover conditions in their medical images and screenings.
Anesthesiologist
An anesthesiologist is a doctor who works with surgeons to give patients anesthesia while in surgery. If anesthesiologists could be a flavor they would be caramel. Since it’s very gentle and smooth and gives you a comforting flavor of sweetness. This is what anesthesiologists give their patients when putting them under anesthesia during their safety medical procedures. To ensure they give their patients comfort like how caramel gives you that sweet comforting flavor.
Hematologist
A hematologist is a specialist who studies the blood organs, and diseases in your blood and treats those diseases. If hematologists could be a flavor they would be raspberry flavored. The deep red color of them represents how hematologists focus and study on blood which is the same color. Raspberries have various tastes, sometimes sour, sweet, and tangy, and that shows how blood has many structured components like raspberries. Raspberries have a strong fierce taste which also shows how important it is when hematologists are working to evaluate and treat blood disorders.
Ophthalmologist
An ophthalmologist is a specific type of eye doctor who gives surgery and eye care. If ophthalmologists were a flavor they would be mint flavored. Mint is a very refreshing, cooling flavor which is how ophthalmologists like to make their patients feel during their visit. When checking their vision patients may have concerns and they relax their patients like how mint has that cooling sense. Mint is a relaxing flavor which is what ophthalmologists like to give their patients if they have any concerns or anxieties about their vision.
Nephrologist
A nephrologist is a specialist who is in the area of treating diseases in your kidneys. If nephrologists could be a flavor they would be blueberry flavored. Blueberries are very high and enriched with antioxidants which help cell damage. Which is what nephrologists do to protect the kidneys’ functions and the antioxidant cells. Blueberries are overall very nourishing to the body just like nephrologists manage to help their patients’ electrolyte levels and kidneys.
Endocrinologist
An endocrinologist is a physician who specifically diagnoses and treats the disorders in your organs and glands that produce your hormones. If endocrinologists were a flavor they would be ginger flavored. Ginger is a complex but strong spicy flavor which shows the balance endocrinologists do to keep the hormone levels in harmony inside the body. Ginger has a cooling and calming inflammatory effect which is what endocrinologists like to provide for their patients. Ginger has many flavor profiles which make it spicy to sweet which shows the complexities of hormonal systems that endocrinologists study.
Oncologist
An oncologist is a physician who is trained in treating and diagnosing an individual with cancer or detecting it. If oncologists were a flavor they would be espresso-flavored. Espresso is a bold powerful flavor which is what oncologists do when dealing with cancer. Espresso has a strong rich flavor which shows the depths and complexity of it. It shows how deep knowledge and perfection they bring to work when dealing with cancer.
Orthopedist
An orthopedist is a medical specialist who focuses on injuries and diseases mainly in the muscles, joints, soft tissues, and bones. If orthopedists were a flavor they would be honey-flavored. Honey is a sweet and soothing flavor that gives reassurance and care. Honey is also in-inflammatory how orthopedists nurture and care for their patients. Honey is a warm color which shows the stability and structure of how orthopedists help patients with their bones and joint stability. Honey is a natural product which is organic and it reflects how the healing under orthopedic care happens.
