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Biological Chemistry Volume 399 Issue 9

Subject Areas: Biochemistry; ;
Publisher: De Gruyter - de Gruyter
ISSN: 1437-4315
SJR: 123

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Frontmatter

2018 Biological Chemistry

doi:10.1515/hsz-2018-frontmatter9
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Highlight: The 7th International Symposium on Kallikreins and Kallikrein-Related Peptidases

Courty, Yves

2018 Biological Chemistry

doi:10.1515/hsz-2018-0326 pmid:30052512
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Manfred Schmitt (1947–2018)

Reuning, Ute; Magdolen, Viktor; Courty, Yves; Clements, Judith A.; Yousef, George M.; Scorilas, Andreas; Talieri, Maroulio; Diamandis, Eleftherios P.

2018 Biological Chemistry

doi:10.1515/hsz-2018-0184 pmid:29601294
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Functional interrelationships between the kallikrein-related peptidases family and the classical kinin system in the human neutrophil

Ehrenfeld, Pamela; Bhoola, Kanti D.; Matus, Carola E.; Figueroa, Carlos D.

2018 Biological Chemistry

doi:10.1515/hsz-2017-0338 pmid:29883315

AbstractIn the human neutrophil, kallikrein-related peptidases (KLKs) have a significant functional relationship with the classical kinin system as a kinin B1 receptor agonist induces secretion of KLK1, KLK6, KLK10, KLK13 and KLK14 into the medium. Secretion of KLK1, the kinin-forming enzyme, may...
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Overview of tissue kallikrein and kallikrein-related peptidases in breast cancer

Figueroa, Carlos D.; Molina, Luis; Bhoola, Kanti D.; Ehrenfeld, Pamela

2018 Biological Chemistry

doi:10.1515/hsz-2018-0111 pmid:29885274

AbstractThe kallikrein family comprises tissue kallikrein and 14 kallikrein-related peptidases (KLKs) recognized as a subgroup of secreted trypsin- or chymotrypsin-like serine proteases. KLKs are expressed in many cellular types where they regulate important physiological activities such as semen...
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Kallikrein-related peptidases in lung diseases

Lenga Ma Bonda, Woodys; Iochmann, Sophie; Magnen, Mélia; Courty, Yves; Reverdiau, Pascale

2018 Biological Chemistry

doi:10.1515/hsz-2018-0114 pmid:29604204

AbstractHuman tissue kallikreins (KLKs) are 15 members of the serine protease family and are present in various healthy human tissues including airway tissues. Multiple studies have revealed their crucial role in the pathophysiology of a number of chronic, infectious and tumour lung diseases....
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The miRNA-kallikrein interaction: a mosaic of epigenetic regulation in cancer

Di Meo, Ashley; Wang, Cong; Cheng, Yufeng; Diamandis, Eleftherios P.; Yousef, George M.

2018 Biological Chemistry

doi:10.1515/hsz-2018-0112 pmid:29604203

AbstractThe kallikrein-related peptidases (KLKs) constitute a family of 15 highly conserved serine proteases with trypsin- and chymotrypsin-like activities. Dysregulated expression and/or aberrant activation of KLKs has been linked to various pathophysiological processes, including cancer. Many...
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Mining human cancer datasets for kallikrein expression in cancer: the ‘KLK-CANMAP’ Shiny web tool

Wang, Chenwei; Moya, Leire; Clements, Judith A.; Nelson, Colleen C.; Batra, Jyotsna

2018 Biological Chemistry

doi:10.1515/hsz-2017-0322 pmid:30052511

AbstractThe dysregulation of the serine-protease family kallikreins (KLKs), comprising 15 genes, has been reportedly associated with cancer. Their expression in several tissues and physiological fluids makes them potential candidates as biomarkers and therapeutic targets. There are several...
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Specificity profiling of human trypsin-isoenzymes

Schilling, Oliver; Biniossek, Martin L.; Mayer, Bettina; Elsässer, Brigitta; Brandstetter, Hans; Goettig, Peter; Stenman, Ulf-Håkan; Koistinen, Hannu

2018 Biological Chemistry

doi:10.1515/hsz-2018-0107 pmid:29883318

AbstractIn humans, three different trypsin-isoenzymes have been described. Of these, trypsin-3 appears to be functionally different from the others. In order to systematically study the specificity of the trypsin-isoenzymes, we utilized proteome-derived peptide libraries and quantitative...
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Activation and activity of glycosylated KLKs 3, 4 and 11

Guo, Shihui; Briza, Peter; Magdolen, Viktor; Brandstetter, Hans; Goettig, Peter

2018 Biological Chemistry

doi:10.1515/hsz-2018-0148 pmid:29975661

AbstractHuman kallikrein-related peptidases 3, 4, 11, and KLK2, the activator of KLK3/PSA, belong to the prostatic group of the KLKs, whose major physiological function is semen liquefaction during the fertilization process. Notably, these KLKs are upregulated in prostate cancer and are used as...

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