The Experts below are selected from a list of 57 Experts worldwide ranked by ideXlab platform

Albert E. Chung - One of the best experts on this subject based on the ideXlab platform.

  • Two distinct cell attachment sites in entactin are revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich epidermal growth factor repeat 2.
    The Journal of biological chemistry, 1995
    Co-Authors: Li-jin Dong, Jyh-cheng Hsieh, Albert E. Chung
    Abstract:

    Abstract The basement membrane glycoprotein, entactin, has previously been shown to promote cell attachment and chemotaxis. We have constructed a panel of glutathione S-transferase fusion proteins that encompasses the four major structural domains of entactin, G1, G2, E, and G3. These proteins have been synthesized in bacteria and purified by affinity chromatography. The Connecting Stalk of entactin, E, which contains four cysteine-rich EGF homology repeats and the integrin receptor RGD recognition sequence, has been modified by deletion of the RGD sequence and substituting glutamic acid for aspartic acid. Attachment assays reveal that the RGD sequence is one of the major cell attachment sites in entactin and that this sequence is recognized by the αβ3 integrin receptor. Analysis of cell attachment on mutant forms of full-length entactin expressed in the baculovirus expression system revealed a second attachment site that was independent of the RGD sequence. This second site was localized to a peptide of 39 amino acid residues in the second globular G2 domain of entactin. This peptide represents a cysteine-rich EGF repeat. Inhibition of cell attachment by anti-integrin receptor antibodies indicates that the second attachment site is recognized by a member of the β1 family of integrin receptors, possibly α3β1.

Li-jin Dong - One of the best experts on this subject based on the ideXlab platform.

  • Two distinct cell attachment sites in entactin are revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich epidermal growth factor repeat 2.
    The Journal of biological chemistry, 1995
    Co-Authors: Li-jin Dong, Jyh-cheng Hsieh, Albert E. Chung
    Abstract:

    Abstract The basement membrane glycoprotein, entactin, has previously been shown to promote cell attachment and chemotaxis. We have constructed a panel of glutathione S-transferase fusion proteins that encompasses the four major structural domains of entactin, G1, G2, E, and G3. These proteins have been synthesized in bacteria and purified by affinity chromatography. The Connecting Stalk of entactin, E, which contains four cysteine-rich EGF homology repeats and the integrin receptor RGD recognition sequence, has been modified by deletion of the RGD sequence and substituting glutamic acid for aspartic acid. Attachment assays reveal that the RGD sequence is one of the major cell attachment sites in entactin and that this sequence is recognized by the αβ3 integrin receptor. Analysis of cell attachment on mutant forms of full-length entactin expressed in the baculovirus expression system revealed a second attachment site that was independent of the RGD sequence. This second site was localized to a peptide of 39 amino acid residues in the second globular G2 domain of entactin. This peptide represents a cysteine-rich EGF repeat. Inhibition of cell attachment by anti-integrin receptor antibodies indicates that the second attachment site is recognized by a member of the β1 family of integrin receptors, possibly α3β1.

Heidi S. Phillips - One of the best experts on this subject based on the ideXlab platform.

  • Molecular Characterization and Distribution of Vascular Endothelial Growth Factor
    Neuroendocrine Perspectives, 1991
    Co-Authors: Napoleone Ferrara, David W. Leung, Heidi S. Phillips
    Abstract:

    The cardiovascular system is the first organ system to develop and reach a functional state in an embryo. This precocity reflects the fundamental role that blood circulation plays in the delivery of nutrients and the disposal of catabolic products in a multicellular organism. Angiogenesis, the growth of new blood vessels, begins in the extraembryonic mesoderm of the yolk sac, the Connecting Stalk and the chorion as early as day 13 in the human (1). Nests of initially isolated endothelial cell cords develop a lumen. Primitive embryonic vessels form by confluence of lumina of separate cords about 2 d later (2,3). Further angiogenesis requires enzymatic degradation of the basement membrane of a local venule (4), endothelial cell Chemotaxis (5) and proliferation (6). Angiogenesis also is required in postnatal life for a wide variety of fundamental physiological processes such as somatic growth, wound healing, tissue and organ regeneration, cyclical growth of the corpus luteum and endometrium. Conversely, uncontrolled angiogenesis is now recognized as an important pathogenic component of a variety of conditions, including rheumatoid arthritis, retinopathies, psoriasis and retrolental fibroplasia (7–9). Also, a major factor that determines potential for rapid growth and propensity to metastasize in tumors is the ability of tumor cells to induce a neovascular response (10). This allows the tumor to establish contact with the vascular bed of the host and to be nourished.

Jyh-cheng Hsieh - One of the best experts on this subject based on the ideXlab platform.

  • Two distinct cell attachment sites in entactin are revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich epidermal growth factor repeat 2.
    The Journal of biological chemistry, 1995
    Co-Authors: Li-jin Dong, Jyh-cheng Hsieh, Albert E. Chung
    Abstract:

    Abstract The basement membrane glycoprotein, entactin, has previously been shown to promote cell attachment and chemotaxis. We have constructed a panel of glutathione S-transferase fusion proteins that encompasses the four major structural domains of entactin, G1, G2, E, and G3. These proteins have been synthesized in bacteria and purified by affinity chromatography. The Connecting Stalk of entactin, E, which contains four cysteine-rich EGF homology repeats and the integrin receptor RGD recognition sequence, has been modified by deletion of the RGD sequence and substituting glutamic acid for aspartic acid. Attachment assays reveal that the RGD sequence is one of the major cell attachment sites in entactin and that this sequence is recognized by the αβ3 integrin receptor. Analysis of cell attachment on mutant forms of full-length entactin expressed in the baculovirus expression system revealed a second attachment site that was independent of the RGD sequence. This second site was localized to a peptide of 39 amino acid residues in the second globular G2 domain of entactin. This peptide represents a cysteine-rich EGF repeat. Inhibition of cell attachment by anti-integrin receptor antibodies indicates that the second attachment site is recognized by a member of the β1 family of integrin receptors, possibly α3β1.

Michael P. Koonce - One of the best experts on this subject based on the ideXlab platform.

  • 25 Å Resolution Structure of a Cytoplasmic Dynein Motor Reveals a Seven-member Planar Ring
    Journal of molecular biology, 2004
    Co-Authors: Montserrat Samsó, Michael P. Koonce
    Abstract:

    Dyneins form one of the three major families of cytoskeleton-based motor proteins that together drive most of the visible forms of cell and organelle movement. We present here a 3D reconstruction of a cytoplasmic dynein motor domain obtained by electron microscopy, at 25 A resolution. This work demonstrates a basic motor architecture of a flat, slightly elliptical ring composed of seven densities arranged around a partially enclosed central cavity. We have used specific Fab tags to localize the microtubule-binding domain; the Connecting Stalk emerges at one end of the motor's long axis. Through proposed fitting of representative AAA domain structures, we show that the nucleotide catalytic P-1 domain is likely located at the opposite end of the motor. Thus mechanisms that couple nucleotide hydrolysis with microtubule binding must be propagated around a ring structure, in a manner clearly distinct from kinesin or myosin-mediated movements. Analysis of the Fab tagged datasets reveals classes of particles with Stalks protruding at distinct angles from the motor. There is a ∼40° variation in microtubule-binding Stalk angle that may reflect linkage to dynein's mechanochemical cycle. Overall, the work provides sufficient resolution to begin the mapping of landmark features onto a dynein motor, and provides a foundation for understanding the mechanics of dynein movement.