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Diagnosis of Leukemia, Lymphoma, and Myeloma
Published in Tariq I Mughal, John M Goldman, Sabena T Mughal, Understanding Leukemias, Lymphomas, and Myelomas, 2017
Tariq I Mughal, John M Goldman, Sabena T Mughal
Nearly all patients with myeloma have an abnormal protein, known as myeloma protein (M protein), in the blood or urine, or both. This is detected by a technique called protein electrophoresis (Fig. 5.25). Most laboratories use a technique called immunofixation to enhance the results of “standard” protein electrophoresis. Immunofixation gives more rapid results than standard protein electrophoresis, and is more sensitive. In most patients, this is of the subtype IgG, followed by IgA, with rare cases of IgM; IgD and IgE are very rare. It is important to note that many diseases are associated with M proteins. These include benign causes, such as monoclonal gammopathy, also known as monoclonal gammopathy of undetermined significance (MGUS). It is, however, important to monitor all patients with M proteins for a progressive rise, which may herald the emergence of myeloma. It is rarely associated with other cancers arising from the lymphatic system, such as CLL and lymphomas. Typically the levels of the M protein are the highest in patients with myeloma. The increased protein can cause a unique phenomenon in the blood, where the red cells appear to be stacked like coins (rouleaux) (Fig. 5.26).
SARS-CoV Infections in Humans
Published in Sunit K. Singh, Human Respiratory Viral Infections, 2014
Protein M is a multiple transmembrane protein. It plays a crucial role during viral assembly and in the budding of virus from the host cells.57,59,63–65 Protein M might also be able to induce interferon responses to infection.66,67
Cytochrome c Oxidase
Published in René Lontie, Copper Proteins and Copper Enzymes, 1984
This has been interpreted either as copper protein impurity or as losses of heme a by detergent action. Since no protein components with an apparent Mr above 36,000 are visible in SDS gels of the best preparations, copper protein impurities must fall in this range of molecular mass or there must be small amounts of copper which bind unspecifically to the enzyme complex. Nevertheless, a value close to 10 nmol/mg protein corresponds to protein Mr near 100,000. The interpretation of this figure on the basis of quantitation of the EPR signals of the resting enzyme, the amount of ligand-reactive heme a, and the minimum Mr of the functional unit leads to the assumption that two Cu atoms are bound in a functional unit with a protein Mr of about 200,000.
Recent trends in next generation immunoinformatics harnessed for universal coronavirus vaccine design
Published in Pathogens and Global Health, 2023
Chin Peng Lim, Boon Hui Kok, Hui Ting Lim, Candy Chuah, Badarulhisam Abdul Rahman, Abu Bakar Abdul Majeed, Michelle Wykes, Chiuan Herng Leow, Chiuan Yee Leow
There are a number of studies that have selected N protein as the target for potential vaccine candidates. In fact, this gene is relatively more conserved and mutationally stable. N proteins of many coronaviruses are highly immunogenic and are abundant during the course of the infection. N protein can also lead to long-lasting immune response without causing any side effect, especially from T-cells. Being the most abundant protein, M protein appears to carry a pivotal role in intracellular budding [82]. High immunogenicity and multifunctional properties of E protein have made itself a promising vaccine target. Significantly, this protein may be directly associated with virulence as indicated by the deletion of this protein led to increased expression of apoptotic markers and elevated virus-induced inflammation in the infected cells [83]. Moreover, as observed from the accumulation of E protein at the ERGIC, this indicates its role in viral assembly and budding [84,85]. Despite minor portion is incorporated eventually into the viral envelope, it has been found that E protein is also participating in virion release [86,87]. On the other hand, many research studies suggest that all structural glycoproteins are considerably involved in viral pathogenesis. A multi-epitope vaccine should thus be designed, to mainly focus on disrupting the life-cycle of coronaviruses.
Efficacy and safety of plasmapheresis without plasma transfusion tandem with chemotherapy to treat multiple myeloma
Published in Hematology, 2022
Yigang Guo, Lulu Zhang, Rongyao Zhang, Meiling Zhou, Xu Chen, Chucheng Wan, Ping Hu, Yuanyuan He, Hua Jiang, Wei Geng, Weixing Zhang, Fariha Kanwal, Muhammad Fayyaz ur Rehman, Zhangzhi Li
Multiple myeloma (MM) [1,2] is the second-largest malignant tumor in the hematological system. Damage of an organ or a tissue due to excessive proliferation of plasma cells coupled with abnormal secretions of monoclonal immunoglobulin (M-Ig) or its para protein fragment (M protein/M spike) is the major cause of its pathogenesis. The majority of MM patients were diagnosed with varying degrees of renal impairment, whereas conditions like hyperviscosity, hyperuricemia, and hypercalcemia tend to aggravate renal injury in some MM patients that were further maintained by hemodialysis. Abnormal components of protein and inflammatory factors can be removed rapidly through plasma exchange that enhances the viscosity of blood and helps reduce organ damage caused by the presence of abnormal protein components and inflammatory factors. Traditional plasmapheresis [3–5] requires a large quantity of fresh frozen plasma. The incidence of an anaphylactic reaction that can be significantly enhanced when a large amount of plasma is utilized substantially limits the application of plasmapheresis in multiple myeloma (MM). Therefore, according to the plasma exchange principle, we pursued a clinical study of sequential chemotherapy [6,7] without plasma exchange to treat patients with newly diagnosed multiple myeloma and achieved good results.
Acute post-streptococcal glomerulonephritis: analysis of the pathogenesis
Published in International Reviews of Immunology, 2021
Jesús Mosquera, Adriana Pedreañez
The M proteins in the bacterial wall have been used for characterizing streptococci. Nephritogenicity is mainly restricted to certain M protein serotypes (ie, 1, 2, 4, 12, 18, 25, 49, 55, 57, and 60) that have shown nephritogenic potential. These may cause skin or throat infections, but specific M types, such as 49, 55, 57, and 60, are most commonly associated with skin infections. However, not all strains of a nephritis-associated M protein serotype are nephritogenic [5]. The relevance of M protein as nephritogenic antigen in APSGN is controversial. This molecule has potential nephritogenic properties. M-protein fractions can complex with fibrinogen and localize in glomeruli [70,71], and glomerulonephritis can be induced with injection of M protein-M protein/fibrinogen complexes [72]. M protein may also be antigenically cross-reactive with the glomerular basement membrane [73] and can act as superantigen inducing M protein-specific Th1-like cells [74]. The capacity of streptococcal M protein type M12/emm12 to induces experimental nephritis by triggering anti-IgG production and enhance renal deposition of IgG and/or immune complexes, has been reported [75]. These mechanisms could have potential relevance to the pathogenesis of APSGN. However, the inconsistent presence of this molecule in renal biopsies from patients with APSGN diminishes its relevance as main nephritogenic antigen. In this regard, Treser et al. [76] have found in glomerular sections of patients with early APSGN that the streptococcal protein is different from the M protein (Figure 3).