Serum enzyme monitoring in sports medicine.

https://aasldpubs.onlinelibrary.wiley.com/doi/pdf/10.1002/hep.1840090518

The liver and IgA: immunological, cell biological and clinical implications.

The aminopeptidases constitute a group of enzymes with closely related activities. In clinical chemistry the analysis of the aminopeptidases and of their multiple forms in serum has for a long time been hindered by considerable confusion concerning their identification, and by a lack of characterization. This is in part due to the often large, and sometimes overlapping substrate specificities of the aminopeptidases. This paper reviews the biochemical properties of the different aminopeptidases, the specificities of the assays used for their analysis in serum, some aspects of their multiple forms--which are especially known to occur for alanine aminopeptidase (EC 3.4.11.2)--and the importance of the determination of aminopeptidases and their multiple forms in clinical chemistry.

/pdf/human-aminopeptidases-a-review-of-the-literature-523lmbap5u.pdf

Human Aminopeptidases: A Review of the Literature

LDH-A, as the critical enzyme accounting for the transformation from pyruvate into lactate, has been demonstrated to be highly expressed in various cancer cells and its silencing has also been approved relating to increased apoptosis in lymphoma cells. In this study, we intend to investigate the correlation between LDH-A and other clinicopathological factors of breast cancer and whether LDH-A silencing could suppress breast cancer growth, and if so the potential mechanisms. 46 breast cancer specimens were collected to study the relation between LDH-A expression and clinicopathological characteristics including menopause, tumor size, node involvement, differentiation, and pathological subtypes classified by ER, PR, and Her-2. shRNAs were designed and applied to silence LDH-A expression in breast cancer cell lines MCF-7 and MDA-MB-231. The effects of LDH-A reduction on cancer cells were studied by a series of in vitro and in vivo experiments, including cell growth assay, apoptosis evaluation, oxidative stress detection, transmission electron microscopy observation, and tumor formation assay on nude mice. LDH-A expression was found to correlate significantly with tumor size and to be independent for other clinicopathological factors. LDH-A reduction resulted in an inhibited cancer cell proliferation, elevated intracellular oxidative stress, and induction of mitochondrial pathway apoptosis. Meanwhile, the tumorigenic ability of LDH-A deficient cancer cells was significantly limited in both breast cancer xenografts. The Ki67 positive cancer cells were significantly reduced in LDH-A deficiency tumor samples, while the apoptosis ratio was enhanced. Our results suggested that LDH-A inhibition might offer a promising therapeutic strategy for breast cancer.

LDH-A silencing suppresses breast cancer tumorigenicity through induction of oxidative stress mediated mitochondrial pathway apoptosis

"Macroenzymes" are enzymes in serum that have formed high-molecular-mass complexes, either by self-polymerization or by association with other serum components. Many enzymes in serum that are measured in clinical chemistry laboratories can occur in a macroenzyme form. Macroenzymes are interesting clinically because of their association with several diseases, including autoimmune diseases and liver disease, and are being investigated as possible diagnostic markers. Most importantly, macroenzymes frequently interfere with the interpretation of serum enzyme results, and as a result can cause diagnostic and therapeutic errors. We review the biochemical characterization, clinical significance, and laboratory detection of macroenzymes.

Macroenzymes: biochemical characterization, clinical significance, and laboratory detection.

Employing the quantitative electrophoretic separation of cytosolic "LAP" activity (EC. 3.4.11.1), the authors investigated the clinical significances of cytosolic and total "LAP" activities in the sera of patients with several different hepatic disorders and elucidated the previously confusing results of aminopeptidase measurements in clinical laboratories. The dominant aminopeptidases measured in human sera by L-leucinamide as substrate are both cytosolic "LAP" and microsomal aminopeptidase (EC. 3.4.11.2). Total "LAP" activity means the sum of these two aminopeptidases. Different substrate specificities are observed in these two enzymes located in other subcellular fractions and different increasing rates of these enzymes are observed in various hepatic diseases. In cases of acute hepatic cell damage, cytosolic "LAP" accounts for a large percentage of total "LAP" of a patient's serum. On the other hand, in cases of elevation of hepatobiliary enzymes, microsomal aminopeptidase constitutes a large part of total "LAP" activity, and the ratio between cytosolic and total "LAP" activity is very low.

Evaluation of cytosolic aminopeptidase in human sera. Evaluation in hepatic disorders.

Characteristics of the complex between alkaline phosphatase and immunoglobulin A in human serum.

Quantitative binding affinities of immunoglobulin G (IgG) for the five isoenzymes of lactate dehydrogenase (LD; EC 1.1.1.27) were determined for IgG isolated from three patients' sera that contained LD-IgG complexes. These three IgGs formed soluble complexes with four (LD 1, 2, 3, 5) of the five LD isoenzymes in two of the patients and in the third they bound with three (LD 2, 3, 4) of the five LD isoenzymes without inhibiting the enzyme activity or precipitating with the enzyme molecules. When rabbit antibody to human IgG was added to these sera, the complexes between the LD isoenzymes and the patients' isolated IgG were completely precipitated. The equilibrium constants for the respective isolated IgG complexes with LD-3 were 0.102, 2.58, and 7.49 X 10(8) L/mol. In these three cases, LD-3 evoked the strongest response from the prepared IgG, demonstrating that the site of antigen recognition of LD-linked IgG was not associated with the structure of individual H and M subunits.

Immunochemical properties of immunoglobulin G conjugated with lactate dehydrogenase

A case of rheumatoid arthritis with various enzyme-immunoglobulin complexes

Low lactate dehydrogenase (LD; EC 1.1.1.27) activity and an abnormal LD pattern in electrophoretograms of LD isoenzymes in the sera of two patients were caused by inhibition of LD by immunoglobulin G. One of these showed inhibitor activity in the serum upon direct analysis, while the other showed activity only after the immunoglobulin was stripped from the LD. As judged from the LD isoenzyme patterns in serum, the LD inhibitor appeared to act against M subunits. However, quantification of binding affinities to each isolated isoenzyme showed that the LD inhibitor had a stronger effect on LD isoenzymes 2 and 3 (H3M1 and H2M2, respectively).

Lactate dehydrogenase inhibition by immunoglobulin G in human serum.

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