1.

Record Nr.

UNINA9910298351203321

Titolo

I Domain Integrins / / edited by Donald Gullberg

Pubbl/distr/stampa

Dordrecht : , : Springer Netherlands : , : Imprint : Springer, , 2014

ISBN

94-017-9153-8

Edizione

[1st ed. 2014.]

Descrizione fisica

1 online resource (188 p.)

Collana

Advances in Experimental Medicine and Biology, , 0065-2598 ; ; 819

Disciplina

572.68

Soggetti

Medicine

Life sciences

Medical genetics

Medical biochemistry

Biomedicine, general

Life Sciences, general

Gene Function

Medical Biochemistry

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.

Nota di bibliografia

Includes bibliographical references and index.

Nota di contenuto

Preface -- 1 Evolution of integrin I domains -- 2 Integrin a1b1 -- 3 Integrin a2b1 -- 4 Integrin a10b1- a collagen receptor critical in skeletal development -- 5 Integrin a11b1 – a major collagen receptor on fibroblastic cells -- 6 Regulation of integrin activity by phosphorylation -- 7 Integrin aEb7:molecular features and functional significance in the immune system -- 8 Structural aspects of integrins -- 9 Integrin recognition motifs in the human collagens -- 10 Cellular signalling by collagen-binding integrins -- 11 The therapeutic potential of I-domain integrins -- Index.

Sommario/riassunto

The integrin family is composed of 24 members and approximately ten years ago (2003) we published a book devoted to the nine I domain integrin subunits. In this second edition, I am pleased that most of the original authors have been able to contribute to the updated version. I domain containing integrins include collagen receptors and leukocyte receptors. In 2003 the knockout mouse phenotypes for all of the I domain integrins had not yet been published; they are now, and are



summarized and discussed in this edition. Interestingly, a recent 10 integrin mutation in dogs has indicated that collagen-binding integrins in the musculoskeletal system might have much more severe phenotypes in larger animals/humans compared to the mild integrin phenotypes observed in collagen-binding integrin deficient mice. This finding is further discussed in the book. In the cancer field, the microenvironment is taking center stage, and here collagen receptors on fibroblasts are predicted to play important roles in paracrine signaling, in regulating tissue stiffness and matrix remodeling. New technologies, new mouse models in combination with analyses of I integrins in larger animals/humans are thus predicted to increase our knowledge about this group of receptors. With this in mind we look forward to another 10 years of research with I domain integrins.