Amyloid P component is located on elastic fibre microfibrils in normal human tissue

Breathnach, S.M.; Melrose, S.M.; Bhogal, B.S.; Beer, Frederick C. de; Dyck, Roland; Tennentt, Glenys; Black, Martin M.; Pepys, Mark B.

doi:10.1038/293652a0

Cited by 192 publications

(67 citation statements)

References 16 publications

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“…I) showed only faint SAP staining along the internal elastic lamina of the artery section, with no visible apoA-I staining. This weak staining is consistent with reports that limited amounts of SAP are found in association with elastic fibers in normal arteries (37). A comparison of immunostaining for SAP and apoE in a normal DIT segment and in a plaque segment is presented in supplementary Fig.…”

Section: Resultssupporting

confidence: 76%

Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications

Stewart

Haw

Lopez

et al. 2007

Journal of Lipid Research

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Serum amyloid P (SAP) is a common component of human amyloid deposits and has been identified in atherosclerotic lesions. We investigated the extent of the colocalization of SAP with apolipoprotein A-I (apoA-I), apoB, apoC-II, and apoE in human coronary arteries and explored potential roles for SAP in these regions, specifically the effect of SAP on the rate of formation and macrophage recognition of amyloid fibrils composed of apoC-II. Analysis of 42 human arterial sections by immunohistochemistry and double label fluorescence microscopy demonstrated that SAP and apoA-I, apoB, apoC-II, and apoE were increased significantly in atherosclerotic lesions compared with nonatherosclerotic segments. SAP colocalized with all four apolipoproteins to a similar extent, whereas plaque macrophages were found to correlate most strongly with apoC-II and apoB. In vitro studies showed that SAP accelerated the formation of amyloid fibrils by purified apoC-II. Furthermore, SAP strongly inhibited the phagocytosis of apoC-II amyloid fibrils by primary macrophages and macrophage cell lines and blocked the resultant production of reactive oxygen species. The ability of SAP to accelerate apoC-II amyloid fibril formation and inhibit macrophage recognition of apoC-II fibrils suggests that SAP may modulate the inflammatory response to amyloid fibrils in

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Section: Resultssupporting

confidence: 76%

Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications

Stewart

Haw

Lopez

et al. 2007

Journal of Lipid Research

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“…Several plasma proteins, including vitronectin, serum amyloid P, and complement components, have been reported to associate with elastic fibers increasingly with age (Dahlbach et al, 1989;Breathnach et al, 1981). The biological significance of the association of these proteins with elastic fibers is not understood.…”

Section: Discussionmentioning

confidence: 99%

The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study.

Roark

Keene²,

Haudenschild³

et al. 1995

J Histochem Cytochem.

180

137

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We examined the pattern of fibulin-1 mRNA and protein expression in human tissues and cell lines. Fibulin-1 transcripts were found in RNA isolated from most tissues and a variety of cultured cells, including fibroblasts, smooth muscle cells, and several epithelial cell lines, but not endothelial cells, lymphomyloid cells, or a number of carcinoma and melanoma lines. Immunohistochemical analysis showed that fibulin-1 is an intercellular component of connective &sues, predominantly associated with matrix fibers in tissues such as the cervix, dermis, intimal and medial layers of blood vessels, heart valves, meningeal tissue of the brain, Wharton's jelly of the umbilical cord, testis, and lung. Most of the fibers that were immunoreactive with fibulin-1 antibodies also stained with antibodies to the elastic fiber proteins elastin

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“…In peripheral tissues, SAP is associated with several ECM proteins, such as elastin in the skin and collagen and laminin in the glomerular basement membrane of the kidney (43)(44)(45)(46)(47)(48). The observation that fibrocytes are evident in experimental wound chambers within days of induction suggests that fibrocytes differentiate quickly after wounding (7,8).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Fibrocyte Differentiation by Serum Amyloid P

Pilling

Buckley

Salmon

et al. 2003

The Journal of Immunology

288

437

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Wound healing and the dysregulated events leading to fibrosis both involve the proliferation and differentiation of fibroblasts and the deposition of extracellular matrix. Whether these fibroblasts are locally derived or from a circulating precursor population is unclear. Fibrocytes are a distinct population of fibroblast-like cells derived from peripheral blood monocytes that enter sites of tissue injury to promote angiogenesis and wound healing. We have found that CD14+ peripheral blood monocytes cultured in the absence of serum or plasma differentiate into fibrocytes within 72 h. We purified the factor in serum and plasma that prevents the rapid appearance of fibrocytes, and identified it as serum amyloid P (SAP). Purified SAP inhibits fibrocyte differentiation at levels similar to those found in plasma, while depleting SAP reduces the ability of plasma to inhibit fibrocyte differentiation. Compared with sera from healthy individuals and patients with rheumatoid arthritis, sera from patients with scleroderma and mixed connective tissue disease, two systemic fibrotic diseases, were less able to inhibit fibrocyte differentiation in vitro and had correspondingly lower serum levels of SAP. These results suggest that low levels of SAP may thus augment pathological processes leading to fibrosis. These data also suggest mechanisms to inhibit fibrosis in chronic inflammatory conditions, or conversely to promote wound healing.

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Amyloid P component is located on elastic fibre microfibrils in normal human tissue

Cited by 192 publications

References 16 publications

Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications

Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications

The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study.

Inhibition of Fibrocyte Differentiation by Serum Amyloid P

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