Enhancement of phagocytosis - A newly found activity of Substance P residing in its N-terminal tetrapeptide sequence

Z. Bar-Shavit; R. Goldman; Y. Stabinsky; P. Gottlieb; M. Fridkin; V. I. Teichberg; S. Blumberg

doi:10.1016/0006-291X(80)90581-1

Enhancement of phagocytosis - A newly found activity of Substance P residing in its N-terminal tetrapeptide sequence

Z. Bar-Shavit^*
, R. Goldman
, Y. Stabinsky
, P. Gottlieb
, M. Fridkin
, V. I. Teichberg
, S. Blumberg

^*Corresponding author for this work

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

276 Scopus citations

Abstract

The undecapeptide Substance P stimulates phagocytosis by mouse macrophages and human polymorphonuclear leukocytes. The activity of Substance P resides in its N-terminal tetrapeptide protion. Substance P and its N-terminal tetrapeptide are as active as tuftsin in their phagocytosis-stimulating activity and compete with tuftsin for its binding sites. The phagocytosis-enhancing activity of Substance P may play a role in inflammatory processes of neural origin where the involvement of the peptide has been implicated.

Original language	English
Pages (from-to)	1445-1451
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	94
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(80)90581-1
State	Published - 30 Jun 1980
Externally published	Yes

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10.1016/0006-291X(80)90581-1

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title = "Enhancement of phagocytosis - A newly found activity of Substance P residing in its N-terminal tetrapeptide sequence",

abstract = "The undecapeptide Substance P stimulates phagocytosis by mouse macrophages and human polymorphonuclear leukocytes. The activity of Substance P resides in its N-terminal tetrapeptide protion. Substance P and its N-terminal tetrapeptide are as active as tuftsin in their phagocytosis-stimulating activity and compete with tuftsin for its binding sites. The phagocytosis-enhancing activity of Substance P may play a role in inflammatory processes of neural origin where the involvement of the peptide has been implicated.",

author = "Z. Bar-Shavit and R. Goldman and Y. Stabinsky and P. Gottlieb and M. Fridkin and Teichberg, \{V. I.\} and S. Blumberg",

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AU - Bar-Shavit, Z.

AU - Goldman, R.

AU - Stabinsky, Y.

AU - Gottlieb, P.

AU - Fridkin, M.

AU - Teichberg, V. I.

AU - Blumberg, S.

PY - 1980/6/30

Y1 - 1980/6/30

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AB - The undecapeptide Substance P stimulates phagocytosis by mouse macrophages and human polymorphonuclear leukocytes. The activity of Substance P resides in its N-terminal tetrapeptide protion. Substance P and its N-terminal tetrapeptide are as active as tuftsin in their phagocytosis-stimulating activity and compete with tuftsin for its binding sites. The phagocytosis-enhancing activity of Substance P may play a role in inflammatory processes of neural origin where the involvement of the peptide has been implicated.

UR - https://www.scopus.com/pages/publications/0018942122

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JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Enhancement of phagocytosis - A newly found activity of Substance P residing in its N-terminal tetrapeptide sequence

Abstract

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