Literature DB >> 2261494

Proteoglycans in haemopoietic cells.

S O Kolset1, J T Gallagher.   

Abstract

Proteoglycans are produced by all types of haemopoietic cells including mature cells and the undifferentiated stem cells. The proteinase-resistant secretory granule proteoglycan (serglycin; Ref. 14), is the most prevalent and best characterised of these proteoglycans. Although its complete pattern of distribution in the haemopoietic system is unknown, serglycin has been identified in the mast cells, basophils and NK cells, in which secretion is regulated, and in HL-60 cells and a monocytoid cell line (Kolset, S.O., unpublished data) in which secretion is constitutive. Proteinase-resistant proteoglycans have been detected in human T-lymphocytes and murine stem cells (FDCP-mix) and the core proteins may be closely related to serglycin. A variety of glycosaminoglycan chains are assembled on the serglycin protein and it is likely that this class of proteoglycan can carry out a wide variety of functions in haemopoietic cells including the regulation of immune responses, inflammatory reactions and blood coagulation. There is strong evidence that in mast cells, NK cells and platelets, the proteoglycans are complexed to basic proteins (including enzymes and cytolytic agents) and amines in secretory granules and such complexes may dissociate following secretion from the cell. The stability of the complexes may be regulated by the ambient pH which may be acidic in the granules and neutral or above in the external medium. However, proteinase-proteoglycan complexes in mast cell granules seem to remain stable after secretion and it has been proposed that the proteoglycan regulates activity of proteinases released into the pericellular domain. The functions of proteoglycans which are constitutively secreted from cells are less clear. If cells have no requirement for storage of basic proteins why do they utilise the same design of proteoglycan as cells which accumulate secretory material prior to regulated release? We should stress that the so-called constitutive secretory pathway has been identified in haemopoietic cells in culture, which are usually maintained and grown in the presence of mitogenic factors (e.g., IL-2, IL-3). the cells are therefore activated and it has not been established that continuous proteoglycan secretion occurs in quiescent cells circulating in the peripheral blood. It is possible that lymphocytes, monocytes and macrophages, in which the constitutive secretion pathway operates in vitro, may store proteoglycan in vivo unless stimulated by mitogens or other activating agents.(ABSTRACT TRUNCATED AT 400 WORDS)

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Year:  1990        PMID: 2261494     DOI: 10.1016/0304-419x(90)90004-k

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  45 in total

Review 1.  Intracellular proteoglycans.

Authors:  Svein Olav Kolset; Kristian Prydz; Gunnar Pejler
Journal:  Biochem J       Date:  2004-04-15       Impact factor: 3.857

2.  Serglycin is a major proteoglycan in polarized human endothelial cells and is implicated in the secretion of the chemokine GROalpha/CXCL1.

Authors:  Astri J Meen; Inger Øynebråten; Trine M Reine; Annette Duelli; Katja Svennevig; Gunnar Pejler; Trond Jenssen; Svein O Kolset
Journal:  J Biol Chem       Date:  2010-11-12       Impact factor: 5.157

Review 3.  Peptide antimicrobial agents.

Authors:  Håvard Jenssen; Pamela Hamill; Robert E W Hancock
Journal:  Clin Microbiol Rev       Date:  2006-07       Impact factor: 26.132

4.  Serglycin proteoglycan is required for multiple myeloma cell adhesion, in vivo growth, and vascularization.

Authors:  Anurag Purushothaman; Bryan P Toole
Journal:  J Biol Chem       Date:  2014-01-08       Impact factor: 5.157

5.  Proteoglycan synthesis in human and murine haematopoietic progenitor cell lines: isolation and characterization of a heparan sulphate proteoglycan as a major proteoglycan from the human haematopoietic cell line TF-1.

Authors:  G Stöcker; Z Drzeniek; U Just; W Ostertag; B Siebertz; H Greiling; H D Haubeck
Journal:  Biochem J       Date:  1996-07-01       Impact factor: 3.857

6.  Proteoglycan synthesis in haematopoietic cells: isolation and characterization of heparan sulphate proteoglycans expressed by the bone-marrow stromal cell line MS-5.

Authors:  Z Drzeniek; B Siebertz; G Stöcker; U Just; W Ostertag; H Greiling; H D Haubeck
Journal:  Biochem J       Date:  1997-10-15       Impact factor: 3.857

Review 7.  Microbial adherence to and invasion through proteoglycans.

Authors:  K S Rostand; J D Esko
Journal:  Infect Immun       Date:  1997-01       Impact factor: 3.441

8.  Hyaluronidase-4 is produced by mast cells and can cleave serglycin chondroitin sulfate chains into lower molecular weight forms.

Authors:  Brooke L Farrugia; Shuji Mizumoto; Megan S Lord; Robert L O'Grady; Rhiannon P Kuchel; Shuhei Yamada; John M Whitelock
Journal:  J Biol Chem       Date:  2019-06-07       Impact factor: 5.157

9.  Proteoglycans in macrophages: characterization and possible role in the cellular uptake of lipoproteins.

Authors:  B Halvorsen; U K Aas; M A Kulseth; C A Drevon; E N Christiansen; S O Kolset
Journal:  Biochem J       Date:  1998-05-01       Impact factor: 3.857

10.  Comparative glycomics of leukocyte glycosaminoglycans.

Authors:  Chun Shao; Xiaofeng Shi; Mitchell White; Yu Huang; Kevan Hartshorn; Joseph Zaia
Journal:  FEBS J       Date:  2013-04-02       Impact factor: 5.542

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