Der Nachweis eines Kreislaufhormons in der Pankreasdrüse. (IV. Mitteilung über dieses Kreislaufhormon.)

Kraut, Heinrich; Frey, E. K.; Werle, E.

doi:10.1515/bchm2.1930.189.3-4.97

Cited by 129 publications

(21 citation statements)

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“…The strong immunoexpression of hK10 by the ducts of the salivary gland is in accordance with the report that almost all kallikreins are expressed by these glands (Diamandis et al 2000b). The discovery of hK1 in the pancreas, salivary glands, and kidney was reported by Werle and his colleagues (Kraut et al 1930;Frey et al 1950). It is well known that there are not only morphological but also functional similarities between the salivary glands, and the pancreas and, except for kallikrein, amylase, glucagon, and peptide P-C are present in both tissues (Ito et al 1983).…”

Section: Discussionmentioning

confidence: 96%

Human Kallikrein 10 Expression in Normal Tissues by Immunohistochemistry

Petraki

Karavana

Luo

et al. 2002

J Histochem Cytochem.

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The normal epithelial cell-specific 1 (NES1) gene (official name kallikrein gene 10, KLK10) was recently cloned and encodes for a putative secreted serine protease (human kallikrein 10, hK10). Several studies have confirmed that hK10 shares many similarities with the other kallikrein members at the DNA, mRNA, and protein levels. The enzyme was found in biological fluids, tissue extracts, and serum. Here we report the first detailed immunohistochemical (IHC) localization of hK10 in normal human tissues. We used the streptavidin-biotin method with two hK10-specific antibodies, a polyclonal rabbit and a monoclonal mouse antibody, developed in house. We analyzed 184 paraffin blocks from archival, current, and autopsy material, prepared from almost every normal human tissue. The staining pattern, the distribution of the immunostaining, and its intensity were studied in detail. Previously, we reported the expression of another novel human kallikrein, hK6, by using similar techniques. The IHC expression of hK10 was generally cytoplasmic and not organ-specific. A variety of normal human tissues expressed the protein. Glandular epithelia constituted the main immunoexpression sites, with representative organs being the breast, prostate, kidney, epididymis, endometrium, fallopian tubes, gastrointestinal tract, bronchus, salivary glands, bile ducts, and gallbladder. The choroid plexus epithelium, the peripheral nerves, and some neuroendocrine organs (including the islets of Langerhans, cells of the adenohypophysis, the adrenal medulla, and Leydig cells) expressed the protein strongly and diffusely. The spermatic epithelium of the testis expressed the protein moderately. A characteristic immunostaining was observed in Hassall's corpuscles of the thymus, oxyphilic cells of the thyroid and parathyroid glands, and chondrocytes. Comparing these results with those of hK6, we observed that both kallikreins had a similar IHC expression pattern.

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Section: Discussionmentioning

confidence: 96%

Human Kallikrein 10 Expression in Normal Tissues by Immunohistochemistry

Petraki

Karavana

Luo

et al. 2002

J Histochem Cytochem.

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“…The study of kallikreins initiated in the 1930s, when Kraut, Frey, and Werle identifi ed a factor of pancreatic ( kallikreas in Greek) extracts able to release the vasoactive decapeptide kallidin (lys-bradikinin) from low-molecular-weight kininogen (Kraut et al , 1930 ;Werle et al , 1937 ). This peptidase was latter named tissue kallikrein (KLK1) to distinguish it from plasma kallikrein (KLKB1), which is secreted by the liver into the circulation and also possesses kininogenase activity.…”

Section: Introductionmentioning

confidence: 99%

Kallikrein-related peptidases in prostate, breast, and ovarian cancers: from pathobiology to clinical relevance

Avgeris

Mavridis

Scorilas

2012

Biological Chemistry

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Tissue kallikrein (KLK1) and kallikrein-related peptidases (KLK2 -15) comprise a family of 15 highly conserved secreted serine proteases with similar structural characteristics and a wide spectrum of functional properties. Both gene expression and protein activity of KLKs are rigorously controlled at various levels via diverse mechanisms, including extensive steroid hormone regulation, to exert their broad physiological role. Nevertheless, deregulated expression, secretion, and function of KLK family members has been observed in several pathological conditions and, particularly, in endocrine-related human malignancies, including those of the prostate, breast, and ovary. The cancer-related abnormal activity of KLKs upon substrates such as growth factors, cell adhesion molecules, cell surface receptors, and extracellular matrix proteins facilitate both tumorigenesis and disease progression to the advanced stages. The well-documented relationship between KLK status and the clinical outcome of cancer patients has led to their identifi cation as promising diagnostic, prognostic, and treatment response monitoring biomarkers for these complex disease entities. The main objective of this review is to summarize the existing knowledge concerning the role of KLKs in prostate, breast, and ovarian cancers and to highlight their continually evolving biomarker capabilities that can provide signifi cant benefi ts for the management of cancer patients.

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“…Human kallikrein-1 (KLK1), the true tissue kallikrein, is responsible for the regulation of blood pressure by cleaving kininogens, thereby displaying a dual tryptic and chymotryptic specificity (Frey and Kraut, 1928;Kraut et al, 1930;Bourgeois et al, 1997;Chao et al, 2006). KLK1 exhibits three sequons of the N-X-S/T type at Asn95, Asn95F and Asn148 (Figure 2).…”

Section: Current Status Of Glyco-klk Site Analysis Tissue Kallikrein mentioning

confidence: 99%

Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity

Guo

Skala

Magdolen

et al. 2014

Biological Chemistry

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Most kallikrein-related peptidases (KLKs) are N-glycosylated with N-acetylglucosamine 2 -mannose 9 units at Asn-Xaa-Ser/Thr sequons during protein synthesis and translocation into the endoplasmic reticulum. These N-glycans are modified in the Golgi machinery, where additional O-glycosylation at Ser and Thr takes place, before exocytotic release of the KLKs into the extracellular space. Sequons are present in all 15 members of the KLKs and comparative studies for KLKs from natural and recombinant sources elucidated some aspects of glycosylation. Although glycosylation of mammalian KLKs 1, 3, 4, 6, and 8 has been analyzed in great detail, e.g., by crystal structures, the respective function remains largely unclear. In some cases, altered enzymatic activity was observed for KLKs upon glycosylation. Remarkably, for KLK3/PSA, changes in the glycosylation pattern were observed in samples of benign prostatic hyperplasia and prostate cancer with respect to healthy individuals. Potential functions of KLK glycosylation in structural stabilization, protection against degradation, and activity modulation of substrate specificity can be deduced from a comparison with other glycosylated proteins and their regulation. According to the new concept of protein sectors, glycosylation distant from the active site might significantly influence the activity of proteases. Novel pharmacological approaches can exploit engineered glycans in the therapeutical context.

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Der Nachweis eines Kreislaufhormons in der Pankreasdrüse. (IV. Mitteilung über dieses Kreislaufhormon.)

Cited by 129 publications

References 0 publications

Human Kallikrein 10 Expression in Normal Tissues by Immunohistochemistry

Human Kallikrein 10 Expression in Normal Tissues by Immunohistochemistry

Kallikrein-related peptidases in prostate, breast, and ovarian cancers: from pathobiology to clinical relevance

Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity

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