Understanding Morris Townsend’s Clinical Course And Complement System Deficiencies

Factors Improving Morris Townsend’s Clinical Outcomes

1. C3 plays a crucial role in the activation of the complement system. Its deficiency causes susceptibility to bacterial infection, (Morgan & Harris, 2015). C3 convertase forms which occur is C4b2b which is formed from the heterodimer in the activated forms of C4 and C2, this enhances the catalysis of the C3 into C3a and C3b. The C3a acts as anaphylatoxin which is the precursor of cytokines which include the ASP and the C3 b acts as opsonizing agent. The cleavage of C3 b into its forms on the patient to C3c and C3d plays a crucial role in B cell response, (Merle, Church, Fremeaux-Bacchi & Roumenina, 2015). The cleaved C3a and C3b on the patients binds covalently pathogens and cell surfaces thus offering protection. This transformation of the patient state improves the clinical outcomes thus improves clinical outcomes.

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2. Factor B is an alternative complement pathway which circulates the blood as single-chain polypeptides. After its activation it is cleaved by complement factor d which complements factor d thus yielding the noncatalytic sub unity of Bp. Bp is involved in the proliferation of preactivated B lymphocytes. Radioactive trace element on factor will; cause radioactive decay on the radio nuclide which has effects on the metabolic reactions. The effect caused leads to increased rates of reactions on the chemicals. Ionization will occur on the C 3 cells causing increased rates of reactions and high rate of cleavage of c3a to c3a and c3b cells. The associated amplification of component activation of c3 b and factor b will yield short-lived convertase of C3bBb, (Nakahira et al., 2011).

3. Serum levels concentrate reflects the different proteins which the plasma are exceptional, which are consumed by the clot formation. Plasma protein accounts for an estimate of about 0.3-0.5g/ L, albumins account for over 50% of total serum in the body and an estimated 75% in colloidal activity, (Haschek, Rousseaux, Wallig, Bolon & Ochoa, 2013). The occurrence of factor 1 deficiency reflects lack of fibrinogen levels. Infusion of pure factor 1 dosage on the parent will correspond with an increase in total serum protein levels on the patient blood profile assessment.

4. Alternative pathways deficiencies have been noted on factor B, D, and properdin. The excess pathway activation on the fluid has been noted with checking on factors H and I. Further factor D deficiency has been noted among twins who suffer respiratory infection shaving H. influenza and Proteus and Pseudomonas spp, (Ram, Lewis & Rice, 2010). Properdin deficiency has been noted among families having X-linked complement deficiency. In this, three types of properdin deficiency have been noted. In type 1 deficiency a deficiency was observed, in type II deficiency, low levels of less than 10% normal levels in serum levels and type II deficiency displaying mutation resulting from impaired properdin binding to C3b, (Fredrikson et al., 1996).

5. The principal analysis in this focus depicts hemagglutination on the patient. The anti C3 aAHG reaction on the C3 coated red blood cells leads to agglutination thus showing that there is a presence of active C3 on the antiglobulin tests which acts as a positive control and negative control for the AHG reactions which lacks the anti C3. This depicts the lack of neutralization of the antic 3 on the patient immune pathway, (Tietze, 2011).

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References:

Merle, N. S., Church, S. E., Fremeaux-Bacchi, V., & Roumenina, L. T. (2015). Complement system part I–molecular mechanisms of activation and regulation. Frontiers in immunology, 6, 262.

Morgan, B. P., & Harris, C. L. (2015). Complement, a target for therapy in inflammatory and degenerative diseases. Nature reviews Drug discovery, 14(12), 857.

Nakahira, K., Haspel, J. A., Rathinam, V. A., Lee, S. J., Dolinay, T., Lam, H. C., … & Fitzgerald, K. A. (2011). Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nature immunology, 12(3), 222.

Haschek, W. M., Rousseaux, C. G., Wallig, M. A., Bolon, B., & Ochoa, R. (Eds.). (2013). Haschek and Rousseaux’s handbook of toxicologic pathology. Academic Press.

Ram, S., Lewis, L. A., & Rice, P. A. (2010). Infections of people with complement deficiencies and patients who have undergone splenectomy. Clinical microbiology reviews, 23(4), 740-780.

Fredrikson, G. N., Westberg, J., Kuijper, E. J., Tijssen, C. C., Sjöholm, A. G., Uhlen, M., & Truedsson, L. (1996). Molecular characterization of properdin deficiency type III: dysfunction produced by a single point mutation in exon 9 of the structural gene causing a tyrosine to aspartic acid interchange. The Journal of Immunology, 157(8), 3666-3671.

Tietze, K. J. (2011). Clinical Skills for Pharmacists-E-Book: A Patient-Focused Approach. Elsevier Health Sciences.

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