Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: KEGG:D03301 (PDL)
 658 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proteoglycan, one of the major non-collagenous protein in the connective tissue, is bound with fibronectin and other cell adhesion proteins, and has a role in the formation of the tissue and the organ. Although the glycosaminoglycan components in various tissue have been widely investigated, the molecular structure of periodontal ligament proteoglycan (PDL-PG) was rarely reported. In present study, proteoglycans of bovine periodontal ligament were purified by chromatography from material adsorbed by DEAE-Sephacel from a guanidium HCl extract. The sequential chromatographic steps consisted of ion-exchange chromatography on DEAE-Sephacel in 4M urea and gel filtration on Sepharose CL-4B in 4M guanidium HCl. The preparation contained a relatively small proteoglycan (Mr = 132,000 dalton) and a free glycosaminoglycan chain (Mr = 88,000 dalton). A Mr = 58,000 dalton core protein was shown by gradient SDS gel electrophoresis after chondroitinase ABC or chondroitinase AC II treatment. The glycosaminoglycan chains after chondroitinase AC II hydrolysis were seen on gel as polydispersed, broad alcian blue staining material (Mr = 20,000-60,000 dalton) while chains were totally hydrolyzed by chondroitinase ABC. These indicate a chondroitin sulfate/dermatan sulate (CS/DS) hybrid glycosaminoglycan chain. Papain digestion of the proteoglycan resulted in a single glycosaminoglycan chain after SDS gel electrophoresis with no protein band. These results suggest that the PDL-PG is slightly larger than that of bone and contains a single chondroitin sulphate/dermatan sulphate chain attached to a 58 K core protein. Antisera raised against PDL-PGs cross-reacted with PDL-PGs but not with other PDL proteins or bone PGs. It has been shown that during biosynthesis of dematan sulfate, L-iduronic acid is formed by epimerization of D-glucuronic acid, and sulfation. The degree of epimerization and sulfation may be related to the function of PDL in buffering the mechanical force applied to the tooth.
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PMID:[Isolation and characterization of proteoglycan in bovine periodontal ligament]. 248 42

Chronic hepatitis C virus (HCV) infection is associated with T-cell exhaustion that is mediated through upregulation of the PD-1 negative regulatory pathway. PD-1 expression is induced by HCV core protein, which also induces upregulation of SOCS-1, a key modulator that controls the Jak/STAT pathway regulating cytokine expression. To determine whether these two negative regulatory pathways are linked during T-cell signaling, SOCS-1 expression was examined by blocking the PD-1 pathway in T cells stimulated with anti-CD3/CD28 in the presence of HCV core protein. T cells isolated from healthy subjects or HCV-infected individuals were treated with anti-PD-1 or anti-PDL-1 antibodies in the presence or absence of HCV core protein, and SOCS-1 gene expression was detected by RT-PCR or immunoblotting, while T-cell functions were assayed by flow cytometric analyses. Both PD-1 and SOCS-1 gene expression were upregulated in healthy T cells exposed to HCV core protein, and blocking the PD-1 pathway downregulated SOCS-1 gene expression in these cells. Additionally, T cells isolated from chronically HCV-infected subjects exhibited increased PD-1 and SOCS-1 expression compared to healthy subjects, and SOCS-1 expression in T cells isolated from HCV-infected subjects was also inhibited by blocking PD-1 signaling; this in turn enhanced the phosphorylation of STAT-1, and improved the impaired T-cell proliferation observed in the setting of HCV infection. These data demonstrate that PD-1 and SOCS-1 are linked in dysregulating T-cell signaling during HCV infection, and their cross-talk may coordinately inhibit T-cell signaling pathways that lead to T-cell exhaustion during chronic viral infection.
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PMID:Programmed death-1 affects suppressor of cytokine signaling-1 expression in T cells during hepatitis C infection. 2088 63