Hylambatins

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Hylambatins

Definition
Hylambatin (Hyl), a dodecapeptide isolated from the skin of the African frog, Hylambates maculatus, belongs to the family of tachykinin or physalaemin-like peptides.

Discovery
It was first isolated from the African rhacophorid frog Hylambates maculates by Yasuhara et al., in the year 19801.

Structural Characteristics
Hyl, a novel tachykinin endecapeptide isolated from the skin of the African frog Hylambates maculatus, must be ascribed to the physalaemin subfamily. It differs structurally from all other known tachykinins mainly in having a methionyl methionine residue at the C-terminus, replacing the usual leucine residue at position 2 from the C-terminal tripeptide -Gly-Leu-Met-NH2 which has been a characteristic feature of all members of the tachykinin family2

Mode of Action
Structure-activity relationship of Hyl and its fragments as studied in the guinea-pig ileum.In a study Hyl and its 12 fragments were tested in the guinea-pig ileum preparation for contractile activities. It was found that all fragments except 3 had contractile activities. The C-terminal fragment as short as the octapeptide sequence was at least as active as the parent molecules. The heptapeptide fragment (Hyl6-12) and the hexapeptide fragment (Hyl7-12) were less active and the C-terminal pentapeptide fragment (Hyl8-12) and the N-terminal hexapeptide fragment (Hyl1-6) were much less active. The N-terminal pentapeptide fragment (Hyl1-5) and the N-terminal fragment from which the N-terminal Asp or Asp-Pro residues were removed (Hyl2-6, Hyl3-6), were inactive at doses used3.

Functions
Hyl, a structurally unique tachykinin: effects on insulin and glucagon secretion: Hyl is the first example of a tachykinin which possesses a methionyl methionine residue at the C-terminus. In a study the effect of Hyl on the secretion of glucoregulatory hormones was examined in the rat. Hyl, injected intravenously in graded doses 10 and 30 min before blood collection. It was found that both plasma glucose and plasma insulin significantly increased, whereas the secretion of glucagon was not affected. This profile of action is different from that of kassinin or substances P, further indicating that Hyl, like other neuropeptides, it may have a role in the regulation of carbohydrate metabolism2.

Parallel bioassay of physalaemin and Hyl on smooth muscle preparations and blood pressure: Hyl, a novel tachykinin endecapeptide isolated from the skin of the African frog Hylambates maculatus, must be ascribed to the physalaemin subfamily. It differs structurally from all other known tachykinins. In parallel bioassay on a number of in-vitro and in-vivo test objects, Hyl and physalaemin were nearly indistinguishable from each other, with few moderate quantitative differences4.

References
1. Yasuhara T, Nakajima T, Falconieri Erspamer G, Erspamer V (1981). New tachykinins Glu2,Pro5-kassinin (Hylambates-kassinin) and hylambatin in the skin of the African rhacophorid frog Hylambates maculatus. Biomed Res., 2:613-617
2. Güllner HG, Harris V, Yajima H, Unger RH (1984). Hylambatin, a structurally unique tachykinin: effects on insulin and glucagon secretion. Arch. Int. Pharmacodyn. Ther., 272(2):304-309.
3. Inoue A, Fukuyasu T, Nakata Y, Yajima H, Nomizu M, Inagaki Y, Asano K, Segawa T (1988). Structure-activity relationship of hylambatin and its fragments as studied in the guinea-pig ileum. J. Pharm. Pharmacol., 40(1):72-73.
4. Falconieri Erspamer G, Mazzanti G, Yasuhara T, Nakajima T (1984). Parallel bioassay of physalaemin and hylambatin on smooth muscle preparations and blood pressure. J. Pharm . Pharmacol., 36(4):284-286.

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Founded in 1984, Bio-Synthesis, Inc. was first known as OCS Laboratories. It was the first producer of commercially available synthetic DNA and, in 1985, became a producer of synthetic peptides. In 1989, OCS incorporated as Bio-Synthesis, Inc. and moved its laboratories to Lewisville, Texas. Today, BSI occupies 10,000 square feet of modern laboratory space (completed in 1995) located 20 miles from downtown Dallas and 10 miles from D/FW airport. Among the surrounding academic institutions are: University of Texas Southwestern Medical School (12 miles), University of North Texas (10 miles), and University of North Texas Health Science Center (25 miles). These universities provide excellent library resources. Since its inception, BSI has steadily expanded its product lines and services to meet the growing needs of the molecular biology community. It has maintained its position as an aggressive, innovative company in a highly competitive marketplace without sacrificing quality. In the beginning, our primary emphasis was on synthesizing high quality DNA primers and linkers, which were the initial uses of oligos. Today, newer technologies, such as gene construction, PCR, mutagenesis, combinatorial libraries, dye/adduct labeling, DNA microarrays, peptide-nucleic acid chimeras, etc. have challenged the molecular biology field. In response, BSI has branched into several related areas including DNA paternity testing, DNA HLA typing, PNA synthesis, genomic sequencing, fluorescence-based genotyping, custom organic synthesis and other molecular biology based applications.

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