Faculty Opinions recommendation of Posttranslational processing of human and mouse urocortin 2: characterization and bioactivity of gene products.

There are 10 known mammalian septin genes, some of which produce multiple splice variants. The current nomenclature for the genes and gene products is very confusing, with several different names having been given to the same gene product and distinct names given to splice variants of the same gene. Moreover, some names are based on those of yeast or Drosophilaseptins that are not the closest homologues. Therefore, we suggest that the mammalian septin field adopt a common nomenclature system, based on that adopted by the Mouse Genomic Nomenclature Committee and accepted by the Human Genome Organization Gene Nomenclature Committee. The human and mouse septin genes will be namedSEPT1–SEPT10 and Sept1–Sept10, respectively. Splice variants will be designated by an underscore followed by a lowercase “v” and a number, e.g., SEPT4_v1.

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Presentation of numerous viral peptides to mouse major histocompatibility complex (MHC) class I-restricted T lymphocytes is mediated by the human MHC-encoded transporter or by a hybrid mouse-human transporter.

Journal of Experimental Medicine ◽

10.1084/jem.177.6.1785 ◽

1993 ◽

Vol 177 (6) ◽

pp. 1785-1790 ◽

Cited By ~ 23

Author(s):

J W Yewdell ◽

F Esquivel ◽

D Arnold ◽

T Spies ◽

L C Eisenlohr ◽

...

Keyword(s):

T Cells ◽

Major Histocompatibility Complex ◽

Antigen Processing ◽

Class I ◽

Gene Products ◽

Major Histocompatibility ◽

Mouse Major Histocompatibility Complex ◽

Histocompatibility Complex ◽

Functional Complex ◽

Human And Mouse

The major histocompatibility complex-encoded transporter associated with antigen processing (TAP) is required for the efficient presentation of cytosolic antigens to class I-restricted T cells. TAP is thought to be formed by the interaction of two gene products, termed TAP1 and TAP2. We find that TAPs consisting either of human subunits, or mouse TAP1 and human TAP2, facilitate the presentation of numerous defined viral peptides to mouse class I-restricted T cells. As human and mouse TAP2 and TAP1 differ in 23 and 28% of their residues, respectively, this indicates that TAP1 and TAP2 can form a functional complex with partners considerably different from those they coevolved with. Moreover, these findings indicate that widely disparate TAPs facilitate delivery of the same peptides to class I molecules. These findings suggest that TAP polymorphism does not greatly influence the types of peptides presented to the immune system.

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Gelatinase (type IV collagenase) immunolocalization in cells and tissues: use of an antiserum to rabbit bone gelatinase that identifies high and low Mr forms

Journal of Cell Science ◽

10.1242/jcs.92.3.487 ◽

1989 ◽

Vol 92 (3) ◽

pp. 487-495 ◽

Cited By ~ 2

Author(s):

G. Murphy ◽

R.M. Hembry ◽

A.M. McGarrity ◽

J.J. Reynolds ◽

B. Henderson

Keyword(s):

Connective Tissue ◽

Polymorphonuclear Leucocytes ◽

Gene Products ◽

Type Iv Collagenase ◽

Type Iv ◽

Rabbit Bone ◽

Tissue Cells ◽

Human And Mouse ◽

Antibody Inhibition

An antiserum was raised to rabbit bone gelatinase (type IV collagenase). It was shown by immunoblotting to detect both the low Mr (72,000) enzyme produced by connective tissue cells from rabbit, pig, human and mouse, as well as the high Mr (94,000-97,000) enzymes secreted by macrophages and polymorphonuclear leucocytes from these species, and by rabbit chondrocytes and endothelial cells. Crossed immunoblotting, antibody inhibition and deglycosylation studies indicated that the high and low Mr forms of gelatinase are immunologically distinct gene products, although their substrate specificity profiles are identical. The anti-gelatinase antiserum was used to immunolocalize the enzyme. Gelatinase was most efficiently detected in rabbit monocytes and connective tissue cells, but cells derived from the human and pig gave poor immunostaining, although mouse gelatinase stained well. The anti-gelatinase antiserum stained cells of the synovial tissue of rabbits at 14 days after induction of an antigen-induced arthritis, demonstrating its usefulness as a tool to assess the role of this enzyme in degradative events.

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Some Structural Features of Metaphase Chromosomes of Mice and Men

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100060969 ◽

1967 ◽

Vol 25 ◽

pp. 190-191

Author(s):

Godfrey C. Hoskins ◽

Betty B. Hoskins

Keyword(s):

Electron Microscopy ◽

Electron Micrographs ◽

Structural Features ◽

Metaphase Chromosomes ◽

The Future ◽

Of Mice And Men ◽

Mouse Cells ◽

Human And Mouse

Metaphase chromosomes from human and mouse cells in vitro are isolated by micrurgy, fixed, and placed on grids for electron microscopy. Interpretations of electron micrographs by current methods indicate the following structural features.Chromosomal spindle fibrils about 200Å thick form fascicles about 600Å thick, wrapped by dense spiraling fibrils (DSF) less than 100Å thick as they near the kinomere. Such a fascicle joins the future daughter kinomere of each metaphase chromatid with those of adjacent non-homologous chromatids to either side. Thus, four fascicles (SF, 1-4) attach to each metaphase kinomere (K). It is thought that fascicles extend from the kinomere poleward, fray out to let chromosomal fibrils act as traction fibrils against polar fibrils, then regroup to join the adjacent kinomere.

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Binucleate Spermiogenesis in the Mouse

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010009381x ◽

1972 ◽

Vol 30 ◽

pp. 112-113

Author(s):

John J. Wolosewick

Keyword(s):

Electron Microscopy ◽

Phosphate Buffer ◽

Seminiferous Epithelium ◽

Mouse Testis ◽

Germinal Epithelium ◽

Intercellular Bridges ◽

Adult Mice ◽

Cervical Dislocation ◽

Human And Mouse

Classically, the male germinal epithelium is depicted as synchronously developing uninucleate spermatids conjoined by intercellular bridges. Recently, binucleate and multinucleate spermatids from human and mouse testis have been reported. The present paper describes certain developmental events in one type of binucleate spermatid in the seminiferous epithelium of the mouse.Testes of adult mice (ABP Jax) were removed from the animals after cervical dislocation and placed into 2.5% glutaraldehyde/Millonig's phosphate buffer (pH 7.2). Testicular capsules were gently split and separated, exposing the tubules. After 15 minutes the tissue was carefully cut into cubes (approx. 1mm), fixed for an additional 45 minutes and processed for electron microscopy.

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Identification of a baculovirus polyhedron formation mutant with a novel phenotype

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100166440 ◽

1996 ◽

Vol 54 ◽

pp. 796-797

Author(s):

James M. Slavicek ◽

Melissa J. Mercer ◽

Mary Ellen Kelly

Keyword(s):

Viral Gene ◽

Gene Products ◽

Type Number ◽

Infection Cycle ◽

Wild Type ◽

Protein Matrix ◽

Insect Midgut ◽

Viral Particles ◽

Budded Virus ◽

Viral Form

Nucleopolyhedroviruses (NPV, family Baculoviridae) produce two morphological forms, a budded virus form and a viral form that is occluded into a paracrystalline protein matrix. This structure is termed a polyhedron and is composed primarily of the protein polyhedrin. Insects are infected by NPVs after ingestion of the polyhedron and release of the occluded virions through dissolution of the polyhedron in the alkaline environment of the insect midgut. Early after infection the budded virus form is produced. It buds through the plasma membrane and then infects other cells. Later in the infection cycle the occluded form of the virus is generated (reviewed by Blissard and Rohrmann, 1990).The processes of polyhedron formation and virion occlusion are likely to involve a number of viral gene products. However, only two genes, the polyhedrin gene and 25K FP gene, have been identified to date that are necessary for the wild type number of polyhedra to be formed and viral particles occluded.

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New insights into heparan sulphate biosynthesis from the study of mutant mice

Biochemical Society Symposium ◽

10.1042/bss0690047 ◽

2002 ◽

Vol 69 ◽

pp. 47-57 ◽

Cited By ~ 8

Author(s):

Catherine L. R. Merry ◽

John T. Gallagher

Keyword(s):

Growth Factors ◽

Biosynthetic Pathway ◽

Heparan Sulphate ◽

Mutant Mice ◽

Gene Products ◽

Multiple Gene ◽

Adhesion Proteins ◽

Ligand Interactions

Heparan sulphate (HS) is an essential co-receptor for a number of growth factors, morphogens and adhesion proteins. The biosynthetic modifications involved in the generation of a mature HS chain may determine the strength and outcome of HS–ligand interactions. These modifications are catalysed by a complex family of enzymes, some of which occur as multiple gene products. Various mutant mice have now been generated, which lack the function of isolated components of the HS biosynthetic pathway. In this discussion, we outline the key findings of these studies, and use them to put into context our own work concerning the structure of the HS generated by the Hs2st-/- mice.

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