BIOSYNTHESIS OF CHONDROITIN SULFATE - MICROSOMAL ACCEPTORS OF SULFATE, GLUCURONIC ACID, AND N-ACETYLGALACTOSAMINE
BIOSYNTHESIS OF CHONDROITIN SULFATE - MICROSOMAL ACCEPTORS OF SULFATE, GLUCURONIC ACID, AND N-ACETYLGALACTOSAMINE
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DOI：
10.1021/bi00744a017
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发表时间：
1973-01-01
期刊：
影响因子：
2.9
通讯作者：
SILBERT, JE
中科院分区：
文献类型：
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作者：
RICHMOND, ME;DELUCA, S;SILBERT, JE
Martha E.里士满，SilvinDeLuca，%和Jeremiah E. Silbert* 摘要：来自鸡胚骨骺软骨的微粒体制剂先前已显示接受[35 S]硫酸盐、[14 C]葡萄糖醛酸和N-[14 C]乙酰半乳糖胺进入内源性糖胺聚糖。内源性糖胺聚糖现在已被进一步表征。在pH6.5时，微粒体制备物与3 ′-磷酸腺苷5 ′-磷酸硫酸盐孵育，硫酸盐掺入内源性6-硫酸软骨素（60-70%）和4-硫酸软骨素（30-40%），而在pH7.8时，只掺入6-硫酸软骨素。在主要是硫酸化的c中，似乎偶尔会掺入非硫酸化的半乳糖胺单位中。关于参与蛋白多糖（硫酸软骨素）的杂多糖（糖胺聚糖）部分合成的中间体，现在已有相当多的信息。尿苷糖核苷酸已被证明是软骨素链的糖的前体（Silbert，1964; Perlman等人，1964），并且用3 '-磷酸腺苷5'-磷酸硫酸盐作为硫酸盐供体证明了新合成的软骨素的显著硫酸化（Silbert和DeLuca，1969）。另外，已经证实，至少一些在细胞外基质中发现的硫酸软骨素杂多糖通过碱不稳定的木糖基-丝氨酸键与蛋白质的丝氨酸单元连接，该键是葡糖醛酸基半乳糖基-半乳糖基-木糖基-丝氨酸蛋白质-多糖“桥”的一部分（Rodén和Smith，1966; Lindahl和Rodén，1966; Helting和Rodén，1968）。尿苷糖核苷酸已被证明是该“桥”合成中的中间体（Helting和Rodén，1969 a，B; Brandt等人，1969; Baker等人，1972年）。或者，有人提出，某些多糖链可能通过一种尚未鉴定的碱稳定键与蛋白质连接（Katalina和Davidson，1966;里昂和Singer，1971）。这可能来自波士顿退伍军人管理医院结缔组织研究实验室以及塔夫茨大学医学院医学系、生物化学和药理学系，波士顿，马萨诸塞州02130。1973年3月6日收到。这项研究得到了美国国家卫生研究所关节炎和代谢疾病研究所AM-08816研究基金的部分支持。已经发表了一份初步报告（里士满等！，1971年）。t现住址：美国国家红十字会，血液研究实验室，马里兰州贝塞斯达。20014.
Martha E. Richmond, Silvana DeLuca,% and Jeremiah E. Silbert* abstract: A microsomal preparation from chick embryo epiphyseal cartilage has previously been shown to accept [35S] sulfate,[14C] glucuronic acid, and/V-[^ acetylgalactos-amine into endogenous glycosaminoglycan. The endogenous glycosaminoglycan has now been characterized further. Incu-bations of microsomalpreparations at pH 6.5 with 3'-phos-phoadenosine 5'-phosphosulfate resulted in incorporation of sulfate into endogenous chondroitin 6-sulfate (60-70%) and chondroitin 4-sulfate (30-40%) while incubations at pH 7.8 resulted inincorporation into chondroitin 6-sulfate ex-clusively. Incorporation appeared to be into occasional non-sulfated galactosamine units in predominantly sulfated c^ Considerable information is now available on the inter-mediates involved in thesynthesis of the heteropolysaccharide (glycosaminoglycan) portion of the proteoglycan, chondroitin sulfate. Uridine sugar nucleotides have been shown to be the precursors for the sugars of the chondroitin chains (Silbert, 1964; Perlman et al., 1964) and significant sulfation of newly synthesized chondroitin (Silbert and DeLuca, 1969) has been demonstrated with 3'-phosphoadenosine 5'-phosphosulfate as sulfate donor. It is also well established that at least some of the chondroitin sulfate heteropolysaccharide found in extra-cellular matrix is linked toserine units of protein by an alkali-labile xylosyl-serine bond which is part of a glucuronosylgalactosyl-galactosyl-xylosyl-serine protein-polysaccharide “bridge”(Rodén and Smith, 1966; Lindahl and Rodén, 1966; Helting and Rodén, 1968). Uridine sugar nucleotides have been shown to be intermediates in the synthesis of this “bridge”(Helting and Rodén, 1969a, b; Brandt et al., 1969; Baker et al., 1972). Alternatively, it has been suggested that some of the polysaccharide chains may be attached to protein by an as yet unidentified bond which is alkali stable (Katsura and Davidson, 1966; Lyons and Singer, 1971). This could t From the Connective Tissue Research Laboratory, Boston Veterans Administration Hospital, and the Departments of Medicine and of Biochemistry and Pharmacology, Tufts University School of Medicine, Boston, Massachusetts 02130. Received March 6, 1973. This investiga-tion was supported in part by Research Grant AM-08816 from the National Institute of Arthritis and Metabolic Diseases, National Insti-tutes of Health. A preliminary report has been published (Richmond eta!., 1971). t Present address: American National Red Cross, Blood Research Laboratory, Bethesda, Md. 20014.