Research article summary (published 2 Sep 2009):

A sulfilimine bond identified in collagen IV.

Full Abstract

Collagen IV networks are ancient proteins of basement membranes that underlie epithelia in metazoa from sponge to human. The networks provide structural integrity to tissues and serve as ligands for integrin cell-surface receptors. They are assembled by oligomerization of triple-helical protomers and are covalently crosslinked, a key reinforcement that stabilizes networks. We used Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules. This bond, the nitrogen analog of a sulfoxide, appears to have arisen at the divergence of sponge and cnidaria, an adaptation of the extracellular matrix in response to mechanical stress in metazoan evolution.

Author information

Author/s: Vanacore, Roberto (R); Ham, Amy-Joan L (AJ); Voehler, Markus (M); Sanders, Charles R (CR); Conrads, Thomas P (TP); Veenstra, Timothy D (TD); Sharpless, K Barry (KB); Dawson, Philip E (PE); Hudson, Billy G (BG);

Affiliation: Division of Nephrology, Department of Medicine and Center for Matrix Biology, Vanderbilt University, Nashville, TN 37232, USA. roberto.vanacore(-atsign-)vanderbilt.edu

Grants: DC007416 (Agency:NIDCD NIH HHS) ; DK065123 (Agency:NIDDK NIH HHS) ; DK18381 (Agency:NIDDK NIH HHS) ; GM059380 (Agency:NIGMS NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't

Journal: Science (New York, N.Y.) (Science), published in United States. (Language: eng)

Reference: 2009-Sep; vol 325 (issue 5945) : pp 1230-4

Dates: Created 2009/09/04; Completed 2009/09/18;

PMID: 19729652, status: MEDLINE (last retrieval date: 9/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amino Acid Sequence Animals Cattle Collagen Type IV - chemistry Humans Hydroxylysine - chemistry Mass Spectrometry Methionine - chemistry Models, Molecular Molecular Sequence Data

Molecular Sequence Data Nitrogen - chemistry Nuclear Magnetic Resonance, Biomolecular Physicochemical Processes Protein Conformation Protein Multimerization Protein Subunits - chemistry Sequence Alignment Stress, Mechanical Sulfur - chemistry

Associated Chemicals: Collagen Type IV (0) ; Protein Subunits (0) ; Hydroxylysine (28902-93-4) ; Methionine (63-68-3) ; Sulfur (7704-34-9) ; Nitrogen (7727-37-9)

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