AGE/RAGE and PKC‐zeta interplay in 3D matrix mediated fibroblast differentiation

Abstract Here, we define an endothelial cell (EC) lumen signaling complex involving Cdc42, Par6b, Par3, junction adhesion molecule (Jam)–B and Jam-C, membrane type 1–matrix metalloproteinase (MT1-MMP), and integrin α2β1, which coassociate to control human EC tubulogenesis in 3D collagen matrices. Blockade of both Jam-B and Jam-C using antibodies, siRNA, or dominant-negative mutants completely interferes with lumen and tube formation resulting from a lack of Cdc42 activation, inhibition of Cdc42-GTP–dependent signal transduction, and blockade of MT1-MMP–dependent proteolysis. This process requires interdependent Cdc42 and MT1-MMP signaling, which involves Par3 binding to the Jam-B and Jam-C cytoplasmic tails, an interaction that is necessary to physically couple the components of the lumen signaling complex. MT1-MMP proteolytic activity is necessary for Cdc42 activation during EC tube formation in 3D collagen matrices but not on 2D collagen surfaces, whereas Cdc42 activation is necessary for MT1-MMP to create vascular guidance tunnels and tube networks in 3D matrices through proteolytic events. This work reveals a novel interdependent role for Cdc42-dependent signaling and MT1-MMP–dependent proteolysis, a process that occurs selectively in 3D collagen matrices and that requires EC lumen signaling complexes, to control human EC tubulogenesis during vascular morphogenesis.

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Service quality function deployment by the C-shaped QFD 3D matrix

Benchmarking An International Journal ◽

10.1108/bij-04-2017-0065 ◽

2018 ◽

Vol 25 (9) ◽

pp. 3386-3405 ◽

Cited By ~ 3

Author(s):

Maryam Hassani ◽

Arash Shahin ◽

Manouchehr Kheradmandnia

Keyword(s):

Quality Function Deployment ◽

Design Methodology ◽

Three Dimensional ◽

Two Dimensional ◽

Customer Requirements ◽

Content Type ◽

Process Characteristics ◽

The Matrix ◽

3D Matrix ◽

Simultaneous Comparison

Purpose The purpose of this paper is to examine the application of C-shaped QFD 3D Matrix in comparing process characteristics (PC), performance aspects (PA) and customer requirements, simultaneously and to prioritize the first two sets, respectively. Design/methodology/approach A three dimensional matrix has been developed with three sets of PC, PA and customers’ requirements and C-shaped matrix has been applied for simultaneous comparison of the dimensions and prioritization of the subsets of PC and PA. The proposed approach has been examined in a post bank. Findings Findings confirm the possibility of simultaneous comparison and prioritization of the three sets of dimensions of this study in post bank services. In addition, “growth and learning” and “bilateral relationship with suppliers” had the first priorities among PA and PC, respectively. Research limitations/implications While the proposed approach has many advantages, filling the matrixes is time-consuming. Since illustrating the 3D matrix was not possible, the matrix was separated into five two-dimensional matrixes. Originality/value Compared to the studied literature, the proposed approach is practically new in the post bank services.

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PKC-lambda is the atypical protein kinase C isoform expressed by immature ventricle

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.1997.272.4.h1636 ◽

1997 ◽

Vol 272 (4) ◽

pp. H1636-H1642

Author(s):

V. O. Rybin ◽

P. M. Buttrick ◽

S. F. Steinberg

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Northern Blot ◽

Blot Analysis ◽

Northern Blot Analysis ◽

Ventricular Myocardium ◽

Adult Rat ◽

Atypical Pkc ◽

Kinase C ◽

Pkc Zeta

We recently identified a developmental decline in protein kinase C (PKC) isoform expression, at the level of the protein, in rat ventricular myocardium. To investigate mechanisms regulating PKC isoform expression in cardiac tissue, this study uses Northern blot analysis to compare the abundance of PKC isoform mRNAs in neonatal and adult rat ventricular myocardium. PKC-epsilon protein and mRNA were detected in both neonatal and adult rat ventricular myocardial preparations. In contrast, coordinate postnatal declines in the abundance of PKC-alpha and PKC-delta proteins and transcripts were identified. An antiserum raised against the COOH-terminal sequence of PKC-zeta detected abundant immunoreactivity in neonatal, but not adult, ventricular myocytes. However, PKC-zeta transcripts were not detectable in the heart either by Northern blot analysis or a reverse transcriptase-polymerase chain reaction approach, indicating that neither the myocytes nor the contaminating cellular elements in the heart express PKC-zeta. Rather, PKC-lambda, another atypical PKC isoform that is structurally highly homologous to PKC-zeta, was detected at the protein and mRNA level in neonatal, but not adult, ventricular myocardium. Taken together, these results establish that developmental declines in calcium-sensitive, novel, and atypical PKC isoforms are paralleled by changes in the levels of the mRNAs encoding these proteins, suggesting transcriptional regulation of PKC during normal cardiac development. The results of this study further identify PKC-lambda as the atypical PKC isoform expressed by the immature ventricle.

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