{"id":185,"date":"2025-05-01T08:55:57","date_gmt":"2025-05-01T08:55:57","guid":{"rendered":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/?p=185"},"modified":"2025-05-01T08:57:10","modified_gmt":"2025-05-01T08:57:10","slug":"immunology","status":"publish","type":"post","link":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/2025\/05\/01\/immunology\/","title":{"rendered":"Immunology"},"content":{"rendered":"\n

Find me a -mAb!<\/strong><\/p>\n\n\n\n

rastuzumab (marketed with the name Herceptin) is a monoclonal antibody that is used
to treat cancer such as: breast cancer, advanced stomach cancer, and advanced cancer in the
gastroesophageal junction. Monoclonal antibodies are proteins that mimic antibodies and
recognize specific target antigens; the target antigens are those that have differences that help
cancer grow. Trastuzumab is used as an injection product, with the injection procedure being to
mix trastuzumab with liquid and inject it into a vein slowly for 30-90 minutes (done at a
hospital)1. There are also some side effects to trastuzumab; some of the side effects include pain
in the muscles, joints, or stomach, hives, itching, flu-like symptoms, redness of the skin, and
even trouble swallowing. Trastuzumab is not the only medication for breast cancer, there are
other such as: Doxorubicin, Epirubicin, Paclitaxel, and more. However unlike other breast cancer
medications offered Trastuzumab specifically treats HER2\/neu proteins. Human epidermal
growth factor (HER2) makes cells divide and grow. Trastuzumab only works if your cancer is
positive for HER2. This means before you start taking the Trastuzumab you will have to consult
a doctor to test your cancer cells to ensure they test positive. If you don’t have an HER2 positive
cancer then Trastuzumab will have no effect on your condition. Once a positive test is procured
Trastuzumab has been shown to be really significant in treating the cancer. Furthermore, it has
been shown through testing to be even better if paired and used in combination with
chemotherapy2.<\/p>\n\n\n\n


Trastuzumab is an IgG1 class antibody<\/p>\n\n\n\n

rastuzumab (marketed with the name Herceptin) is a monoclonal antibody that is used
to treat cancer such as: breast cancer, advanced stomach cancer, and advanced cancer in the
gastroesophageal junction. Monoclonal antibodies are proteins that mimic antibodies and
recognize specific target antigens; the target antigens are those that have differences that help
cancer grow. Trastuzumab is used as an injection product, with the injection procedure being to
mix trastuzumab with liquid and inject it into a vein slowly for 30-90 minutes (done at a
hospital)1. There are also some side effects to trastuzumab; some of the side effects include pain
in the muscles, joints, or stomach, hives, itching, flu-like symptoms, redness of the skin, and
even trouble swallowing. Trastuzumab is not the only medication for breast cancer, there are
other such as: Doxorubicin, Epirubicin, Paclitaxel, and more. However unlike other breast cancer
medications offered Trastuzumab specifically treats HER2\/neu proteins. Human epidermal
growth factor (HER2) makes cells divide and grow. Trastuzumab only works if your cancer is
positive for HER2. This means before you start taking the Trastuzumab you will have to consult
a doctor to test your cancer cells to ensure they test positive. If you don’t have an HER2 positive
cancer then Trastuzumab will have no effect on your condition. Once a positive test is procured
Trastuzumab has been shown to be really significant in treating the cancer. Furthermore, it has
been shown through testing to be even better if paired and used in combination with
chemotherapy2.
Trastuzumab is an IgG1 class antibody<\/p>\n\n\n\n

<\/p>\n\n\n\n

\"\"<\/a><\/figure>\n\n\n\n

Trastuzumab works by specifically targeting the HER2 protein, and attaching to it5.
Trastuzumab works by binding to the outer surface of cancer cells that have the receptor human
epidermal growth protein factor 2(HER2)5. In many HER2 positive cancers HER2 plays a
critical role in growth and division which can lead to a surplus in growth and tumor expansion.
Trastuzumab binds to the HER2 protein and blocks its ability for HER2 to send growth signals to
the cancer cells. This blockage stops the cancer cells from proliferating making trastuzumab an
effective answer to HER2 proteins. Furthermore, trastuzumab can also trigger antibody-
dependent cellular cytotoxicity (ADCC)3. ADCC is An immune response where immune cells,
like natural killer (NK) cells, destroy a target cell that has antibodies attached to it. The NK cells
recognize the antibodies on the target cell and kill it3. Additionally, it also disrupts angiogenesis
which is the process of new blood vessels forming from already existing ones4. This is important
because it stops preventing angiogenesis trastuzumab stunts the tumor growth by limiting its
source for natural resources needed to survive like oxygen. The limiting of tumor resources can
also lead to a reduction in the size of the tumor; which can ultimately lead to a reduction in some
of the symptoms an afflicted individual may experience. It is through all of these processes and
procedures that Trastuzumab is able to prevent the growth and success of HER2 receptors having
cancer cells, which will ultimately lead to a positive outcome for the afflicted patient.<\/p>\n\n\n\n

REFERENCES
1 Trastuzumab. (Herceptin) | Cancer information | Cancer Research UK. (2024, November
14). https:\/\/www.cancerresearchuk.org\/about-cancer\/treatment\/drugs\/trastuzumab
2 McKeage, K., & Perry, C. M. (2002). Trastuzumab: a review of its use in the treatment
of metastatic breast cancer overexpressing HER2. Drugs, 62(1), 209\u2013243.
https:\/\/doi.org\/10.2165\/00003495-200262010-00008
3 Collins, D. M., O’Donovan, N., McGowan, P. M., O’Sullivan, F., Duffy, M. J., &
Crown, J. (2012). Trastuzumab induces antibody-dependent cell-mediated cytotoxicity (ADCC)
in HER-2-non-amplified breast cancer cell lines. Annals of oncology : official journal of the
European Society for Medical Oncology, 23(7), 1788\u20131795.
https:\/\/doi.org\/10.1093\/annonc\/mdr484
4 \u2013Gajria, D., & Chandarlapaty, S. (2011). HER2-amplified breast cancer: mechanisms
of trastuzumab resistance and novel targeted therapies. Expert review of anticancer therapy,
11(2), 263\u2013275. https:\/\/doi.org\/10.1586\/era.10.226
5 Nahta, R., & Esteva, F. J. (2006). HER2 therapy: molecular mechanisms of
trastuzumab resistance. Breast cancer research : BCR, 8(6), 215.
https:\/\/doi.org\/10.1186\/bcr1612<\/p>\n\n\n\n

DRAW igM<\/mark><\/strong><\/p>\n\n\n\n

The IgM-BCR structure is different from the soluble pentameric igM in several ways;
This paragraph will highlight some of these differences. In glycosylation in IgM-BCR there are
14 sites that are present in IgM-BCR located at; ECDa(Asn57, Asn63, Asn73, Asn88, Asn97,
and Asn112), ECDb (Asn73 and Asn101). And then Three additional glycosylation sites are
located on each heavy chain: (Asn 332, Asn 395, Asn 402). .This is different from pentameric
IgM glycosylation sites which are located on the heavy chain at five locations: Asn-171, Asn-
332, Asn-395, Asn-402, and Asn-563. Furthermore, it is believed that the spread of glycosylation
sites on Igm-BCR makes patches that are free of sites. Fab regions of the IgM pentameric exhibit
some form of flexibility at the Cu2-Cu3. This is different from the BCR-IgM which still is more
rigid but still has some flexibility relative to the Fc domain. Another difference is that in BCR-
IgM the Fab Regions aren’t visible which is thought to be caused by the structural flexibility. The
structure of the Pentameric IgM appears to be star fish. With a Joining chain (J-Chain) which
regulates the structure. The BCR-IgM appears to be closer to a Y shape which resembles the
replication fork. Another difference is Soluble pentameric Igm is secreted, and BCR-Igm is
considered membrane bound.
In my drawing of the IgM-BCR structure included a total of 14 glycosylation sites; 6 ad
ECDa, 2 at ECDb and 3 on each heavy chain. There were also 4 Constant regions; Cu1, Cu2,
Cu3, Cu4. FaB regions were near the top. The membrane spanning region was at the bottom of
the structure and was composed of a Transmembrane region notably TMua and TMub.<\/p>\n\n\n\n

\"\"<\/a><\/figure>\n\n\n\n
\"\"<\/a><\/figure>\n\n\n\n

End-of-term reflection<\/strong><\/p>\n\n\n\n

One of the most valuable things I learned in this immunology class was how the immune system detects and responds to pathogens through processes like antigen presentation and cytokine signaling. This knowledge greatly enhanced my understanding of microbiology, especially when studying how various microbes either evade or trigger immune responses in the human body. It helped me grow as a student by strengthening my critical thinking and ability to make connections across subjects. It did get a little confusing with the memorizing all the different cytokines and immune functions. however, Learning how innate and adaptive immune systems interact helped me better understand the host pathogen dynamics we explored in microbiology labs. Immunology provided a framework to interpret how specific infections can lead to systemic effects. this will be an insight that will be essential in my future career as a pathologist. A strong grasp of immune mechanisms is key to making accurate diagnoses of immune related diseases and infections. With my pathologist career in mind, this course has been especially valuable. Not only has it helped me make connections across my current coursework, but its also knowledge I know I will continue to apply throughout my career. <\/p>\n","protected":false},"excerpt":{"rendered":"

Find me a -mAb! rastuzumab (marketed with the name Herceptin) is a monoclonal antibody that is usedto treat cancer such as: breast cancer, advanced stomach cancer, and advanced cancer in thegastroesophageal junction. Monoclonal antibodies are proteins that mimic antibodies andrecognize… Continue Reading →<\/a><\/p>\n","protected":false},"author":28366,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":"","wds_primary_category":0},"categories":[1],"tags":[],"_links":{"self":[{"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/posts\/185"}],"collection":[{"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/users\/28366"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/comments?post=185"}],"version-history":[{"count":2,"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/posts\/185\/revisions"}],"predecessor-version":[{"id":191,"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/posts\/185\/revisions\/191"}],"wp:attachment":[{"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/media?parent=185"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/categories?post=185"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/sites.wp.odu.edu\/dr-steele-the-cool-cat\/wp-json\/wp\/v2\/tags?post=185"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}