Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity最新文献_第3页

The effect of pituitary adenylate cyclase activating polypeptide (PACAP) on amylase secretion from guinea pig pancreatic acini. 垂体腺苷酸环化酶激活多肽(PACAP)对豚鼠胰腺腺泡淀粉酶分泌的影响。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

M Kitagawa, S Naruse, H Ishiguro, T Hayakawa, K Nokihara

{"title":"The effect of pituitary adenylate cyclase activating polypeptide (PACAP) on amylase secretion from guinea pig pancreatic acini.","authors":"M Kitagawa, S Naruse, H Ishiguro, T Hayakawa, K Nokihara","doi":"","DOIUrl":"","url":null,"abstract":"Pituitary adenylate cyclase activating polypeptide (PACAP) is a novel hypothalamic peptide, structurally related to vasoactive intestinal peptide (VIP). Our previous study in conscious dogs revealed that PACAP stimulated exocrine pancreatic secretion in a manner different from VIP. The objectives of this study were to characterize the effects of PACAP on amylase secretion and intracellular cAMP production in guinea pig pancreatic acini and to compare them with those of VIP and secretin. PACAP38 and PACAP27 (10(-10)-10(-8)M) stimulated amylase secretion from pancreatic acini in a concentration-related manner. The order of potency for amylase secretion was PACAP27 = VIP > PACAP38. The maximally stimulated amylase secretion by PACAP27 was not enhanced by VIP or secretin, but was synergistically increased by cholecystokinin and A23187. PACAP38 and PACAP27 (10(-2)-10(-7)M) increased intracellular cAMP levels in a concentration-related manner. The potency for cAMP production was PACAP38 = PACAP27 = VIP. These results suggest that PACAP38 and PACAP27, like VIP, directly stimulate amylase secretion from guinea pig pancreatic acini through alterations in cellular cAMP levels.","PeriodicalId":8980,"journal":{"name":"Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity","volume":"1 2","pages":"73-6"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20278416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Solid phase synthesis and immunogenicity of a VP3 peptide from hepatitis A virus. 甲型肝炎病毒VP3肽的固相合成及其免疫原性。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

J A Pérez, J F González-Dankaart, F Reig, R M Pintó, A Bosch, I Haro

引用次数: 0

Recombinant epithelial cell mucin (MUC-1) expressed in baculovirus resembles antigenically tumor associated mucin, target for cancer immunotherapy. 杆状病毒表达的重组上皮细胞粘蛋白(muc1)是肿瘤免疫治疗的靶点。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

P Ciborowski, O J Finn

引用次数: 0

Cleavage of a beta-amyloid precursor sequence by cathepsin D. 组织蛋白酶D切割β -淀粉样蛋白前体序列。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

B M Austen, D J Stephens

引用次数: 0

Synthesis, purification and biological activity of (Ser10-phosphatidyl)-urodilatin (phosphourodilatin). (丝氨酸-磷脂酰)-尿扩张素的合成、纯化及生物活性研究。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

H Mostafavi, K Adermann, S Austermann, M Raida, M Meyer, W G Forssmann

{"title":"Synthesis, purification and biological activity of (Ser10-phosphatidyl)-urodilatin (phosphourodilatin).","authors":"H Mostafavi, K Adermann, S Austermann, M Raida, M Meyer, W G Forssmann","doi":"","DOIUrl":"","url":null,"abstract":"Based on the global phosphorylation approach, a selective synthesis of (Ser10-phosphatidyl)-urodilatin (phosphourodilatin), which contains 32 amino acid residues and a disulfide loop is described. The peptide was assembled stepwise on a polyethyleneglycol-polystyrene support using Fmoc-chemistry. The phosphorylation was performed on-resin by phosphitylation with a large excess of di-tert-butyl-N,N-diethylphosphoramidite within 1 hour, followed by oxidation with tert-butylhydroperoxide to the protected phosphopeptide. After cleavage and deprotection the disulfide bridge was introduced without side reactions by iodine titration of the mono-acetamidomethyl protected crude peptide. During the synthetic pathway, the acylation with side chain-unprotected Fmoc-serine and the phosphitylation satisfactorily yielded the expected intermediates. In some phosphorylation experiments a by-product having a reduced mass corresponding to the H-phosphonate was observed. Illustrated with the synthesis of phosphourodilatin, this type of by-product, which could not be separated by HPLC, and the difficult amino acid sequence make the synthesis of a large phosphopeptide a more delicate task than the synthesis of short phosphopeptides, which do not contain oxidation-sensitive amino acids, difficult sequences or additional structural elements such as disulfide loops. The biological activity of phosphourodilatin was compared with non-phosphorylated urodilatin in two assay systems. Both peptides revealed a vasorelaxant effect on aortic smooth muscle strips and induced a cGMP-generation in RFL-6 cells with increasing dose dependency.","PeriodicalId":8980,"journal":{"name":"Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity","volume":"1 5","pages":"255-60"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20496140","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The intracellular assembly of antigenic-peptide-class II complexes. II类抗原肽复合物的细胞内组装。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

S K Pierce, J M Green, A E Faassen, X Xu, W Song, H Cho, P Schafer, T Psaradellis, N Wagle, J Kim

{"title":"The intracellular assembly of antigenic-peptide-class II complexes.","authors":"S K Pierce, J M Green, A E Faassen, X Xu, W Song, H Cho, P Schafer, T Psaradellis, N Wagle, J Kim","doi":"","DOIUrl":"","url":null,"abstract":"The immune system employs remarkable strategies to ensure that foreign antigens, from the most complex pathogens to the simplest proteins, are displayed on the surfaces of cells which are targets of T lymphocyte recognition. At the heart of these strategies is the molecular transformation of a soluble protein antigen to a complex of a small peptide containing the antigenic determinant bound to a cell surface Major Histocompatibility Complex class I or class II protein. This process is termed antigen presentation. Progress in a variety of laboratories over the last several years has yielded a wealth of information about the molecular mechanisms underlying antigen presentation, providing potential new approaches to vaccine design. Here we describe recent studies in our laboratory aimed at elucidating the intracellular site in B lymphocytes in which antigenic peptide-class II complexes are assembled for recognition by helper T cells and the regulation of this assembly process. Our results suggest that processed antigen-class II complexes are assembled in a unique compartment in the endocytic route which contains all the necessary cellular and molecular machinery for assembly and that B cells regulate the assembly process in response to external and internal signals.","PeriodicalId":8980,"journal":{"name":"Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity","volume":"1 3","pages":"149-56"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20278520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural effects of glycosylation on the C-terminal pentapeptide of peptide T. 糖基化对肽T c端五肽的结构影响。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

K V Prammer, L Otvos

引用次数: 0

In vitro and in vivo comparison of a randomly coupled antibody fragment-enzyme conjugate with a site-specific conjugate. 体外和体内随机偶联抗体片段-酶偶联物与位点特异性偶联物的比较。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

R C Werlen, R E Offord, D C Blakey, S J East, R G Melton, K Rose

引用次数: 0

Synthesis, solution structure and biological action of PACAP-related peptide. pacap相关肽的合成、溶液结构及生物学作用。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

V Wray, K Nokihara, S Naruse, E Ando, C Kakoschke, M Wei

引用次数: 0

Synthetic antigenic peptides as a new strategy for immunotherapy of cancer. 合成抗原肽作为肿瘤免疫治疗的新策略。

Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity Pub Date : 1995-01-01

E Appella, D J Loftus, K Sakaguchi, A Sette, E Celis

{"title":"Synthetic antigenic peptides as a new strategy for immunotherapy of cancer.","authors":"E Appella, D J Loftus, K Sakaguchi, A Sette, E Celis","doi":"","DOIUrl":"","url":null,"abstract":"Antigens presented by class I of the major histocompatibility complex (MHC) are recognised by the T cell receptor of CD8+ cytolytic effector cells (CTLs), while class II molecules present antigens to CD4+ helper T cells. For both class I and class II molecules, structure and function are linked through the binding of peptides. Consensus or individual sequences have been obtained for naturally processed peptides bound to a variety of class I and class II molecules, revealing the general features of peptides associated with MHC molecules. The interactions between peptides and MHC molecules have been more clearly defined by the characterization of the three dimensional structure of several different MHC molecules. CTLs have been implicated in immune responses against tumors and it is now well documented that some human tumors express specific antigens, which are recognised by CTLs and could potentially be used in immunotherapy protocols. The use of antigenic peptides to elicit a specific and effective CTL response in vivo offers several advantages over the use of other antigenic moieties. Emerging strategies for the safe and effective administration of peptides to humans may lead to their use in the immunological prevention and treatment of cancer.","PeriodicalId":8980,"journal":{"name":"Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity","volume":"1 3","pages":"177-84"},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20278524","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0