PubMed Health⌕ Search

PubMed · 11022978

Capillary network patterning during angiogenesis.

Abstract

1. Although much is known of signalling events associated with angiogenesis, starting with a sprout, less is known of how an intact microvascular network is correctly formed following the initiation of sprouting. The aim of the present report is to evaluate some of the factors that could be involved in directing the patterning of the resulting microvascular bed. 2. Hypothetical 'patterning rules' are discussed and considered in the context of data obtained from studies of angiogenesis. The guidelines suggest that both tissue- and stimulus-specific regulators are involved in directing patterning. 3. Examples of 'patterned' and 'non-patterned' angiogenesis in rat mesentery are given, with evidence to support stimulus-related differences in angiogenesis patterns. 4. Skeletal muscle angiogenesis follows metabolic patterns within the muscle, as discerned through traditional histochemical evaluation. However, further examination, using confocal microscopy and new patterning assays, indicates that branching patterns differ according to stimulus. Patterning guidelines within the tissue may be important in preventing the growth of sinusoidal vessels. 5. The concept of 'angiotypes' is proposed to direct future studies towards understanding how therapeutic angiogenesis or angiostasis applications can be used to obtain correctly patterned microvascular networks. Angiogenesis via 'branching' compared with 'non-branching' angiotypes will involve different signalling pathways. Both sprouting and dividing of capillaries are found in the 'branching' angiotype, with each pattern having several subtypes that would be expected to be mediated via different signalling mechanisms.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

F M Hansen-Smith. 2000. Capillary network patterning during angiogenesis.. https://doi.org/10.1046/j.1440-1681.2000.03341.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Capillary array electrophoresis-MALDI mass spectrometry using a vacuum deposition interface.

We previously introduced a vacuum deposition interface for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF MS) on a moving surface (e.g., quartz wheel, Mylar tape, metal target). In our present work, the approach has been extended to demonstrate parallel analysis for multiple on-line infusion MALDI MS and capillary array electrophoresis (CAE)-MALDI MS. In the infusion mode, individual peptide samples were simultaneously deposited on a Mylar tape cartridge using an array of eight capillaries, yielding eight parallel traces. For CAE-MALDI/TOF MS, the same number of separation capillaries were coupled with an array of eight infusion capillaries using a common liquid junction, containing matrix solution. A fast-scanning mirror was employed to traverse the beam of the desorption laser across the Mylar tape to probe one trace at a time. The positions of the eight sample traces formed on the tape were automatically determined, and all samples were analyzed in rapid sequence using a kilohertz repetition rate laser and a high-throughput data acquisition system. The instrumentation was operated with CAE MS for high-throughput analysis without compromising data quality. The principles of parallel separation-vacuum deposition should be generally applicable to MALDI/TOF MS analysis for proteomics and other areas where separation and high throughput are required.

Angiotensins↗

Extracellular matrix molecules, long-term potentiation, memory consolidation and the brain angiotensin system.

Considerable evidence now suggests an interrelationship among long-term potentiation (LTP), extracellular matrix (ECM) reconfiguration, synaptogenesis, and memory consolidation within the mammalian central nervous system. Extracellular matrix molecules provide the scaffolding necessary to permit synaptic remodeling and contribute to the regulation of ionic and nutritional homeostasis of surrounding cells. These molecules also facilitate cellular proliferation, movement, differentiation, and apoptosis. The present review initially focuses on characterizing the ECM and the roles of cell adhesion molecules (CAMs), matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs), in the maintenance and degradation of the ECM. The induction and maintenance of LTP is described. Debate continues over whether LTP results in some form of synaptic strengthening and in turn promotes memory consolidation. Next, the contribution of CAMs and TIMPs to the facilitation of LTP and memory consolidation is discussed. Finally, possible roles for angiotensins, MMPs, and tissue plasminogen activators in the facilitation of LTP and memory consolidation are described. These enzymatic pathways appear to be very important to an understanding of dysfunctional memory diseases such as Alzheimer's disease, multiple sclerosis, brain tumors, and infections.

Angiotensins↗

Angiotensin AT(1) receptor stimulates heat shock protein 27 phosphorylation in vitro and in vivo.

The angiotensin type 1 receptor (AT(1)) exerts a variety of its signaling and cellular actions through its effects on protein phosphorylation. Phosphoproteomic analysis of angiotensin (Ang) II-stimulated aortic smooth muscle cells revealed that heat shock protein 27 (HSP27) represents a major protein phosphorylation target of the AT(1) signaling pathway. Stimulation of cells with Ang II resulted in 1.7-fold (P<0.05) and 5.5-fold (P<0.001) increases in HSP27 phosphoisoforms at pI 5.7 and pI 5.4, respectively. This was accompanied by a 54% (P<0.01) decrease in the nonphosphorylated HSP27 isoform, located at pI 6.4. Treatment of samples with alkaline phosphatase reversed this redistribution of HSP27 phosphoisoforms. Ang II-stimulated HSP27 phosphorylation was completely blocked by pretreatment of cells with the AT(1) antagonist CV11974. Phosphoamino acid analysis demonstrated that Ang II-induced phosphorylation of both HSP27 phosphoisoforms occurred exclusively on serine. Protein kinase C inhibition completely blocked phorbol ester-induced HSP27 phosphorylation but did not impair Ang II-stimulated phosphorylation of HSP27, suggesting that AT(1) increased HSP27 phosphorylation by a protein kinase C-independent pathway. Intrajugular infusion of Ang II in rats increased HSP27 in aorta by 1.7-fold (P<0.02), and this response was inhibited by CV11974. These results suggest that Ang II-induced HSP27 phosphorylation is a physiologically relevant AT(1) signaling event. Because serine phosphorylation of HSP27 blocks its ability to cap F-actin, Ang II/AT(1)-induced HSP27 phosphorylation may play a key role in actin filament remodeling required for smooth muscle cell migration and contraction.

Angiotensins↗