Analysis of atrial natriuretic factor biosynthesis and secretion in adult and neonatal rat atrial cardiocytes.
Analysis of atrial natriuretic factor biosynthesis and secretion in adult and neonatal rat atrial cardiocytes.
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成年和新生大鼠心房心肌细胞心房钠尿因子生物合成和分泌的分析。
DOI：
10.1016/0024-3205(87)90748-x
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发表时间：
1987
期刊：
影响因子：
6.1
通讯作者：
Graham,RM
中科院分区：
文献类型：
--
作者：
Zisfein,JB;Sylvestre,D;Homcy,CJ;Graham,RM
心房利钠因子（ANF）作为126个氨基酸的多肽proANF储存在心房心肌细胞中，其随后裂解为24-28个氨基酸的羧基末端肽，即主要的循环形式。早期的研究已经证明，分离的、培养的新生大鼠心肌细胞储存并分泌proANF，其可以被血清蛋白酶切割成较小的循环形式。由于新生大鼠和成年大鼠心肌细胞在心钠素合成和加工方面可能存在差异，我们比较了新生大鼠心肌细胞和成年大鼠心肌细胞储存和分泌的心钠素的形式。用新生大鼠和成年大鼠的离体心房肌细胞培养4 ~ 5天，用35 S-半胱氨酸和35 S-蛋氨酸进行脉冲追踪研究。通过使用针对proANF的羧基末端或氨基末端的抗体对细胞提取物和培养基进行免疫沉淀，然后进行SDS-PAGE和放射自显影，对这些细胞储存和分泌的ANF进行分析。发现成人和新生儿培养物的细胞提取物仅含有一种17 kDa的多肽，此前被鉴定为proANF。在培养基中发现的主要形式也是17-kDa肽，其3-kDa羧基末端和14-kDa氨基末端裂解产物的数量较少。我们从这些研究中得出结论，proANF是成人和新生儿心肌细胞在培养中储存和分泌的主要形式;在这些培养物中，将proANF切割成循环中发现的较小形式的蛋白酶的活性要么减弱，要么被高ANF分泌率所淹没。或者，ANF加工和分泌途径可能在培养物中以某种方式改变，使得proANF逃避蛋白酶切割。进一步的研究将阐明这种蛋白酶的性质和位置。
Atrial natriuretic factor (ANF) is stored in atrial cardiocytes as the 126 amino acid polypeptide, proANF, which is later cleaved to the 24–28 amino acid carboxyterminal peptides, the major circulating forms. Earlier studies have demonstrated that isolated, cultured neonatal rat cardiocytes both store and secrete proANF, which can be cleaved to the smaller circulating form(s) by a serum protease. Since differences may exist between neonatal and adult cardiocytes with respect to ANF synthesis and processing, we compared the forms of ANF stored and secreted by neonatal rat cardiocytes with those of adult cells. Using four to five day cultures of isolated atrial cardiocytes prepared from the hearts of neonatal and adult rats, pulse-chase studies were performed with35S-cysteine and35S-methionine. Analysis of ANF stored and secreted by these cells was performed by immunoprecipitation of cell extracts and culture media using antibodies directed to either the carboxyterminus or aminoterminus of proANF followed by SDS-PAGE and autoradiogarphy. Cell extracts from both adult and neonatal cultures were found to contain only a 17-kDa polypeptide, previously identified as proANF. The predominant form found in the culture media was also the 17-kDa peptide, with smaller quantities of its 3-kDa carboxyterminal and 14-kDa aminoterminal cleavage products. We conclude from these studies that proANF is the major form stored and secreted by both adult and neonatal cardiocytes in culture; the activity of the protease that cleaves proANF to the smaller forms found in the circulation is either attenuated or is overwhelmed by high ANF-secretory rates in these cultures. Alternatively, the ANF processing and secretory pathways may be somehow altered in culture such that proANF escapes protease cleavage. Further studies will elucidate the nature and location of this protease.
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影响因子：
56.9
作者：
R. Sparkes;MC Sparkes;M. Wilson;JW Towner;W. Benedict;A. Murphree;J. Yunis
通讯作者：
R. Sparkes;MC Sparkes;M. Wilson;JW Towner;W. Benedict;A. Murphree;J. Yunis
Pro α 2(I) 胶原蛋白基因中的单碱基突变导致 RNA 从外显子 27 到外显子 29 的有效剪接，并合成缩短但符合读框的 Pro α 2(I) 链。
DOI：
--
发表时间：
1988
影响因子：
11.1
作者：
G. Tromp;D. Prockop
通讯作者：
D. Prockop
影响因子：
56.9
作者：
DYSON, N;HOWLEY, PM;HARLOW, E
通讯作者：
HARLOW, E
影响因子：
64.8
作者：
LEE, WH;SHEW, JY;LEE, EYHP
通讯作者：
LEE, EYHP
影响因子：
56.9
作者：
SPARKES, RS;MURPHREE, AL;BENEDICT, WF
通讯作者：
BENEDICT, WF