Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer

Carolina Proaño-Bolaños; Renjie Li; Mei Zhou; Lei Wang; Xinping Xi; Elicio E. Tapia; Luis A. Coloma; Tianbao Chen; Chris Shaw

doi:10.1016/j.euprot.2017.02.001

Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer

Carolina Proaño-Bolaños
, Renjie Li
, Mei Zhou
, Lei Wang
, Xinping Xi
, Elicio E. Tapia
, Luis A. Coloma
, Tianbao Chen
, Chris Shaw

Life sciences Faculty

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Peptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern C-X₍₇₎-C-X_(6,7)-C-X_(6,7)-Y-X₍₃₎-C-X₍₂₎-C-X_(15-21)-C and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These peptidase inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions.

Original language	English
Pages (from-to)	1-13
Number of pages	13
Journal	EuPA Open Proteomics
Volume	15
DOIs	https://doi.org/10.1016/j.euprot.2017.02.001
State	Published - 1 Jun 2017

Bibliographical note

Publisher Copyright:
© 2017 The Authors

Keywords

Cruziohyla calcarifer
Frog skin secretion
Kazal-type proteinase inhibitors
Molecular cloning
Peptidomic
Tandem mass spectrometry

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10.1016/j.euprot.2017.02.001

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title = "Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer",

abstract = "Peptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern C-X(7)-C-X(6,7)-C-X(6,7)-Y-X(3)-C-X(2)-C-X(15-21)-C and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These peptidase inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions.",

keywords = "Cruziohyla calcarifer, Frog skin secretion, Kazal-type proteinase inhibitors, Molecular cloning, Peptidomic, Tandem mass spectrometry",

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note = "Publisher Copyright: {\textcopyright} 2017 The Authors",

year = "2017",

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day = "1",

doi = "10.1016/j.euprot.2017.02.001",

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T1 - Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer

AU - Proaño-Bolaños, Carolina

AU - Li, Renjie

AU - Zhou, Mei

AU - Wang, Lei

AU - Xi, Xinping

AU - Tapia, Elicio E.

AU - Coloma, Luis A.

AU - Chen, Tianbao

AU - Shaw, Chris

PY - 2017/6/1

Y1 - 2017/6/1

N2 - Peptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern C-X(7)-C-X(6,7)-C-X(6,7)-Y-X(3)-C-X(2)-C-X(15-21)-C and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These peptidase inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions.

AB - Peptidase inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern C-X(7)-C-X(6,7)-C-X(6,7)-Y-X(3)-C-X(2)-C-X(15-21)-C and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These peptidase inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions.

KW - Cruziohyla calcarifer

KW - Frog skin secretion

KW - Kazal-type proteinase inhibitors

KW - Molecular cloning

KW - Peptidomic

KW - Tandem mass spectrometry

UR - https://www.scopus.com/pages/publications/85016956554

U2 - 10.1016/j.euprot.2017.02.001

DO - 10.1016/j.euprot.2017.02.001

M3 - Artículo

AN - SCOPUS:85016956554

SN - 2212-9685

VL - 15

SP - 1

EP - 13

JO - EuPA Open Proteomics

JF - EuPA Open Proteomics

ER -

Novel Kazal-type proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer

Abstract

Bibliographical note

Keywords

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