The C1q inhibitor in serum is a chondroitin 4-sulfate proteoglycan.

Silvestri, L; Baker, John; Rodén, Lennart; Stroud, Robert M.

doi:10.1016/s0021-9258(19)68974-x

Cited by 69 publications

(14 citation statements)

References 33 publications

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“…protein. We estimated the molecular mass of the P.PG protein core to be 20-27 kDa depending on the deglycosylation method used before SDS/ polyacrylamide-gel-electrophoretic analysis; this value fits rather well with calculated values for the molecular mass of the core from data of Silvestri et al [6] and Okayama et al [7] (16-20 kDa). On the other hand the amino acid composition of the isolated P.PG in the present work is in good agreement with the data of Okayama et al [7], suggesting that the P.PG that we have isolated is identical with their preparation.…”

Section: Discussionsupporting

confidence: 78%

“…P.PG was characterized as containing polydisperse molecules, the polydispersity being due to variations in the d,grees of glycosylation and presumably sulphatation. Silvestri et al [6] reported the polydispersity of a chondroitin 4-sulphate platelet proteoglycan with molecular masses ranging from 45 to 750 kDa (average value 175 kDa) containing 9 % protein. Okayama et al [7] characterized a platelet proteoglycan (molecular mass 136 kDa), presumably identical with the former, with four chondroitin 4-sulphate side chains and containing 15 %.…”

Section: Discussionmentioning

confidence: 99%

“…The P.PG might therefore be a platelet factor 4 carrier for delivery to sites of blood-vessel injury. An inhibitor of complement subcomponent Clq has been identified in human serum as to be proteoglycan [6]. On the basis of the nature and the size of their glycosaminoglycan side chains, the proteoglycans involved in these two functions might be related despite the fact that average molecular masses appeared to be somewhat different; this observation could be the result of partial degradation during the preparations.…”

Section: Introductionmentioning

confidence: 99%

“…This P.PG was very similar to the Clq inhibitor previously characterized. It is therefore likely that P.PG acts as a Clq inhibitor in addition to being a carrier of platelet factor 4 [5][6][7]. Despite the importance of the two above-mentioned biological roles, a molecular study of P.PG protein core is still lacking.…”

Section: Introductionmentioning

confidence: 99%

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Characterization and N-terminal sequence of human platelet proteoglycan

Périn

Bonnet

Maillet

et al. 1988

Biochemical Journal

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Human platelet proteoglycan (P.PG) was prepared from a 4 M-guanidinium chloride platelet extract in the presence of proteinase inhibitors. The purification procedure included CsCl-density-gradient centrifugation, DEAE-Sepharose CL-6B ion-exchange chromatography and f.p.l.c. on a Mono Q HR 5/5 column. P.PG was recovered as a polydisperse molecule, but the protein core appeared to be at least 90% homogeneous. This observation could be due to partial proteolysis of the core protein during extraction. The N-terminal sequence of the human P.PG core protein was determined up to residue 66 and was shown to be highly homologous to the propeptide of an embryonic rat yolk-sac tumour proteoglycan (PG19); the significance of this homology is discussed.

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Section: Discussionsupporting

confidence: 78%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization and N-terminal sequence of human platelet proteoglycan

Périn

Bonnet

Maillet

et al. 1988

Biochemical Journal

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“…This interpretation is complicated by the discovery that certain glial scar components (such as specific CSPG subtypes [117,118]), and the glial scar as a whole [119][120][121], both appear to facilitate axon regeneration and neurite outgrowth. Additionally, disruption of injury-induced astrocyte responses upstream of scar formation impedes recovery by impairing injury containment, BBB repair, and inflammation resolution [121][122][123][124], and astrocytes themselves may adopt multiple reactive phenotypes that likely exist on a functional spectrum [44,125] and that may, in turn, be influenced by proteoglycans [123,126]. Whatever new findings future studies may hold, it is clear that the ECM has a profound influence on brain health and disease.…”

Section: Microglia and The Extracellular Matrix In Health And Diseasementioning

confidence: 99%

Microglia as hackers of the matrix: sculpting synapses and the extracellular space

et al. 2021

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Microglia shape the synaptic environment in health and disease, but synapses do not exist in a vacuum. Instead, pre- and postsynaptic terminals are surrounded by extracellular matrix (ECM), which together with glia comprise the four elements of the contemporary tetrapartite synapse model. While research in this area is still just beginning, accumulating evidence points toward a novel role for microglia in regulating the ECM during normal brain homeostasis, and such processes may, in turn, become dysfunctional in disease. As it relates to synapses, microglia are reported to modify the perisynaptic matrix, which is the diffuse matrix that surrounds dendritic and axonal terminals, as well as perineuronal nets (PNNs), specialized reticular formations of compact ECM that enwrap neuronal subsets and stabilize proximal synapses. The interconnected relationship between synapses and the ECM in which they are embedded suggests that alterations in one structure necessarily affect the dynamics of the other, and microglia may need to sculpt the matrix to modify the synapses within. Here, we provide an overview of the microglial regulation of synapses, perisynaptic matrix, and PNNs, propose candidate mechanisms by which these structures may be modified, and present the implications of such modifications in normal brain homeostasis and in disease.

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Protein a treatment of cancer: Activation of a serum component with trans‐species anti‐B16 melanoma activity

Cooper

Masinello

1983

Intl Journal of Cancer

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Mice (C57BL) succumbed to cultured B16 melanoma cells i.p. with reproducible kinetics and an MST2 of about 26 days. Serum from tumour-bearing or normal mice was treated at 0 degree C with fixed SAC cells and injected i.p. into fresh tumour-bearing mice. If serum was given 7 days or less after B16 inoculation, the MST of the mice was highly significantly increased by up to 32%. Similar activity has been generated in normal human, rabbit and guinea-pig serum, while untreated sera were ineffective. Apparently the sera contained an inactive native precursor that was activated by the SAC to produce an anti-tumour agent. Precursor and product were both relatively labile at 0 degree C. Anti-tumour activity was eluted at pH 2.5 from SAC or Sepharose-protein-A pretreated with serum, thus implicating the protein A component of SAC. The eluates contained haemolytically active C1, the first component of complement, and five crude C1 preparations made by standard methods showed good anti-tumour activity. However, seven other highly haemolytic C1 preparations had no anti-tumour effect. Similarly, two crude preparations of the subcomponent C1q had good anti-tumour activity, but eight other, more pure and highly haemolytic C1q preparations were inactive in mice. Thus the anti-tumour principle was not C1 or C1q alone, although it had some chemical properties in common with these substances. It remains unidentified, but has potential interest for cancer therapy.

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The C1q inhibitor in serum is a chondroitin 4-sulfate proteoglycan.

Cited by 69 publications

References 33 publications

Characterization and N-terminal sequence of human platelet proteoglycan

Characterization and N-terminal sequence of human platelet proteoglycan

Microglia as hackers of the matrix: sculpting synapses and the extracellular space

Protein a treatment of cancer: Activation of a serum component with trans‐species anti‐B16 melanoma activity

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