30 July 1940 CHAVES County Specimen Collection Data

Specimen collected 30 July 1940. Original Locality: Rio Felix 1 mi. above Highway 285. Locality: Rio Felix 1 mi. above Highway 285.Catalog number: MSB130; Taxa: Lepomis cyanellus; Common name: green sunfish; Count of specimens: 20; Standard length:Catalog number: MSB203; Taxa: Micropterus salmoides; Common name: largemouth bass; Count of specimens: 7; Standard length:Catalog number: MSB245; Taxa: Lepomis megalotis; Common name: longear sunfish; Count of specimens: 34; Standard length:Catalog number: MSB258; Taxa: Lepomis megalotis; Common name: longear sunfish; Count of specimens: 111; Standard length:Catalog number: MSB389; Taxa: Ictalurus lupus; Common name: headwater catfish; Count of specimens: 4; Standard length:Catalog number: MSB428; Taxa: Ameiurus melas; Common name: black bullhead; Count of specimens: 26; Standard length:Catalog number: MSB481; Taxa: Ictalurus punctatus; Common name: channel catfish; Count of specimens: 1; Standard length:Catalog number: MSB563; Taxa: Fundulus zebrinus; Common name: plains killifish; Count of specimens: 59; Standard length:Catalog number: MSB645; Taxa: Pimephales promelas; Common name: fathead minnow; Count of specimens: 2; Standard length:Catalog number: MSB832; Taxa: Micropterus salmoides; Common name: largemouth bass; Count of specimens: 2; Standard length:Catalog number: MSB1014; Taxa: Fundulus zebrinus; Common name: plains killifish; Count of specimens: 1; Standard length:Catalog number: MSB1093; Taxa: Gambusia affinis; Common name: western mosquitofish; Count of specimens: 1; Standard length:Catalog number: MSB1096; Taxa: Gambusia affinis; Common name: western mosquitofish; Count of specimens: 1; Standard length:Catalog number: MSB1120; Taxa: Hybognathus amarus; Common name: Rio Grande silvery minnow; Count of specimens: 62; Standard length:Catalog number: MSB1137; Taxa: Hybognathus amarus; Common name: Rio Grande silvery minnow; Count of specimens: 3; Standard length:Catalog number: MSB1156; Taxa: Hybognathus amarus; Common name: Rio Grande silvery minnow; Count of specimens: 52; Standard length:Catalog number: MSB1314; Taxa: Cyprinella lutrensis; Common name: red shiner; Count of specimens: 2; Standard length:Catalog number: MSB1335; Taxa: Cyprinella lutrensis; Common name: red shiner; Count of specimens: 104; Standard length:Catalog number: MSB1354; Taxa: Cyprinella lutrensis; Common name: red shiner; Count of specimens: 633; Standard length:Catalog number: MSB1565; Taxa: Cyprinus carpio; Common name: common carp; Count of specimens: 56; Standard length:Catalog number: MSB1575; Taxa: Cyprinus carpio; Common name: common carp; Count of specimens: 4; Standard length:Catalog number: MSB1704; Taxa: Dionda episcopa; Common name: roundnose minnow; Count of specimens: 35; Standard length:Catalog number: MSB1709; Taxa: Dionda episcopa; Common name: roundnose minnow; Count of specimens: 1533; Standard length:Catalog number: MSB1862; Taxa: Macrhybopsis aestivalis; Common name: speckled chub; Count of specimens: 2; Standard length:Catalog number: MSB1965; Taxa: Dorosoma cepedianum; Common name: gizzard shad; Count of specimens: 3; Standard length:Catalog number: MSB1975; Taxa: Dorosoma cepedianum; Common name: gizzard shad; Count of specimens: 18; Standard length:Catalog number: MSB2189; Taxa: Astyanax mexicanus; Common name: Mexican tetra; Count of specimens: 2; Standard length:Catalog number: MSB2194; Taxa: Astyanax mexicanus; Common name: Mexican tetra; Count of specimens: 34; Standard length:Catalog number: MSB2198; Taxa: Astyanax mexicanus; Common name: Mexican tetra; Count of specimens: 18; Standard length:Catalog number: MSB2215; Taxa: Dionda episcopa; Common name: roundnose minnow; Count of specimens: 107; Standard length:Catalog number: MSB2718; Taxa: Ictalurus lupus; Common name: headwater catfish; Count of specimens: 43; Standard length:Catalog number: MSB2868; Taxa: Lepomis macrochirus; Common name: bluegill ; Count of specimens: 4; Standard length:Catalog number: MSB3202; Taxa: Carpiodes carpio; Common name: river carpsucker; Count of specimens: 48; Standard length:Catalog number: MSB3210; Taxa: Carpiodes carpio; Common name: river carpsucker; Count of specimens: 79; Standard length:Catalog number: MSB3398; Taxa: Lepisosteus osseus; Common name: longnose gar; Count of specimens: 1; Standard length:Catalog number: MSB3446; Taxa: Cyprinodon pecosensis; Common name: Pecos pupfish; Count of specimens: 3; Standard length:Catalog number: MSB13100; Taxa: Notropis stramineus; Common name: sand shiner; Count of specimens: 45; Standard length

Protector and friend: Turning points and discursive constructions of the stepparent role

Objective: To understand turning points (TPs) in the development of positive stepparent–stepchild communication and relationships. Background: Scholars stress the importance of communication in co-constructing healthy stepparent–stepchild relationships. The researchers focused on positive stepparenting via understanding transformational turning point (TP) events across time. Research questions explored how stepparents with an overall positive relationship with a stepchild characterize TPs and the discursive constructions of the stepparent role. Method: The team analyzed 877 pages of data from 37 in-depth interviews with stepparents who described self-identified TP events, reflected in visual graphs of 279 TPs. Results: Data were coded into 11 TP types, focused on structural and role changes for stepparents, co-constructed over time. The top three TP types were changes in household composition, communicating support through offering protection and being present/available, and role change, most frequently by functioning as a parent versus friend. All the TPs highlight discursive work to forge positive stepparenting roles. Conclusions: The findings extend earlier studies of stepchildren’s experiences and communication practices that ground resilience to manage relational resources through investments of quality time and enactment of social support. Implications: Applications suggest support for stepparents to have quality interactions with stepchildren and training to develop healthy communication practices and facilitate resilience

Application of remote sensor data to geologic analysis of the Bonanza test site Colorado

Research activities on geologic remote sensing applications for Colorado are summarized. Projects include: regional and detailed geologic mapping, surficial and engineering geology, fracture studies, uranium exploration, hydrology, and data reduction and enhancement. The acquisition of remote sensor data is also discussed

Muscular Dystrophy-Associated SUN1 and SUN2 Variants Disrupt Nuclear-Cytoskeletal Connections and Myonuclear Organization

Proteins of the nuclear envelope (NE) are associated with a range of inherited disorders, most commonly involving muscular dystrophy and cardiomyopathy, as exemplified by Emery-Dreifuss muscular dystrophy (EDMD). EDMD is both genetically and phenotypically variable, and some evidence of modifier genes has been reported. Six genes have so far been linked to EDMD, four encoding proteins associated with the LINC complex that connects the nucleus to the cytoskeleton. However, 50% of patients have no identifiable mutations in these genes. Using a candidate approach, we have identified putative disease-causing variants in the SUN1 and SUN2 genes, also encoding LINC complex components, in patients with EDMD and related myopathies. Our data also suggest that SUN1 and SUN2 can act as disease modifier genes in individuals with co-segregating mutations in other EDMD genes. Five SUN1/SUN2 variants examined impaired rearward nuclear repositioning in fibroblasts, confirming defective LINC complex function in nuclear-cytoskeletal coupling. Furthermore, myotubes from a patient carrying compound heterozygous SUN1 mutations displayed gross defects in myonuclear organization. This was accompanied by loss of recruitment of centrosomal marker, pericentrin, to the NE and impaired microtubule nucleation at the NE, events that are required for correct myonuclear arrangement. These defects were recapitulated in C2C12 myotubes expressing exogenous SUN1 variants, demonstrating a direct link between SUN1 mutation and impairment of nuclear-microtubule coupling and myonuclear positioning. Our findings strongly support an important role for SUN1 and SUN2 in muscle disease pathogenesis and support the hypothesis that defects in the LINC complex contribute to disease pathology through disruption of nuclear-microtubule association, resulting in defective myonuclear positioning

Requirements for Efficient Proteolytic Cleavage of Prelamin A by ZMPSTE24

The proteolytic maturation of the nuclear protein lamin A by the zinc metalloprotease ZMPSTE24 is critical for human health. The lamin A precursor, prelamin A, undergoes a multi-step maturation process that includes CAAX processing (farnesylation, proteolysis and carboxylmethylation of the C-terminal CAAX motif), followed by ZMPSTE24-mediated cleavage of the last 15 amino acids, including the modified C-terminus. Failure to cleave the prelamin A "tail", due to mutations in either prelamin A or ZMPSTE24, results in a permanently prenylated form of prelamin A that underlies the premature aging disease Hutchinson-Gilford Progeria Syndrome (HGPS) and related progeroid disorders.Here we have investigated the features of the prelamin A substrate that are required for efficient cleavage by ZMPSTE24. We find that the C-terminal 41 amino acids of prelamin A contain sufficient context to allow cleavage of the tail by ZMPSTE24. We have identified several mutations in amino acids immediately surrounding the cleavage site (between Y646 and L647) that interfere with efficient cleavage of the prelamin A tail; these mutations include R644C, L648A and N650A, in addition to the previously reported L647R. Our data suggests that 9 of the 15 residues within the cleaved tail that lie immediately upstream of the CAAX motif are not critical for ZMPSTE24-mediated cleavage, as they can be replaced by the 9 amino acid HA epitope. However, duplication of the same 9 amino acids (to increase the distance between the prenyl group and the cleavage site) impairs the ability of ZMPSTE24 to cleave prelamin A.Our data reveals amino acid preferences flanking the ZMPSTE24 cleavage site of prelamin A and suggests that spacing from the farnesyl-cysteine to the cleavage site is important for optimal ZMPSTE24 cleavage. These studies begin to elucidate the substrate requirements of an enzyme activity critical to human health and longevity

Quantitative nucleolar proteomics reveals nuclear re-organization during stress- induced senescence in mouse fibroblast

<p>Abstract</p> <p>Background</p> <p>Nucleolus is the most prominent mammalian organelle within the nucleus which is also the site for ribosomal biogenesis. There have been many reports indicating the involvement of nucleolus in the process of aging. Several proteins related to aging have been shown to localize in the nucleolus, which suggests the role of this organelle in senescence.</p> <p>Results</p> <p>In this study, we used quantitative mass spectrometry to map the flux of proteins into and out of the nucleolus during the induction of senescence in cultured mammalian cells. Changes in the abundance of 344 nucleolar proteins in sodium butyrate-induced senescence in NIH3T3 cells were studied by SILAC (stable isotope labeling by amino acids in cell culture)-based mass spectrometry. Biochemically, we have validated the proteomic results and confirmed that B23 (nucleophosmin) protein was down-regulated, while poly (ADP-ribose) polymerase (PARP) and nuclear DNA helicase II (NDH II/DHX9/RHA) were up-regulated in the nucleolus upon treatment with sodium butyrate. Accumulation of chromatin in the nucleolus was also observed, by both proteomics and microscopy, in sodium butyrate-treated cells. Similar observations were found in other models of senescence, namely, in mitoxantrone- (MTX) treated cells and primary fibroblasts from the Lamin A knockout mice.</p> <p>Conclusion</p> <p>Our data indicate an extensive nuclear organization during senescence and suggest that the redistribution of B23 protein and chromatin can be used as an important marker for senescence.</p

LAP2 Is Widely Overexpressed in Diverse Digestive Tract Cancers and Regulates Motility of Cancer Cells

BACKGROUND: Lamina-associated polypeptides 2 (LAP2) is a nuclear protein that connects the nuclear lamina with chromatin. Although its critical roles in genetic disorders and hematopoietic malignancies have been described, its expression and roles in digestive tract cancers have been poorly characterized. METHODS: To examine the expression of LAP2 in patient tissues, we performed immunohistochemistry and real-time PCR. To examine motility of cancer cells, we employed Boyden chamber, wound healing and Matrigel invasion assays. To reveal its roles in metastasis in vivo, we used a liver metastasis xenograft model. To investigate the underlying mechanism, a cDNA microarray was conducted. RESULTS: Immunohistochemistry in patient tissues showed widespread expression of LAP2 in diverse digestive tract cancers including stomach, pancreas, liver, and bile duct cancers. Real-time PCR confirmed that LAP2β is over-expressed in gastric cancer tissues. Knockdown of LAP2β did not affect proliferation of most digestive tract cancer cells except pancreatic cancer cells. However, knockdown of LAP2β decreased motility of all tested cancer cells. Moreover, overexpression of LAP2β increased motility of gastric and pancreatic cancer cells. In the liver metastasis xenograft model, LAP2β increased metastatic efficacy of gastric cancer cells and mortality in tested mice. cDNA microarrays showed the possibility that myristoylated alanine-rich C kinase substrate (MARCKS) and interleukin6 (IL6) may mediate LAP2β-regulated motility of cancer cells. CONCLUSIONS: From the above results, we conclude that LAP2 is widely overexpressed in diverse digestive tract cancers and LAP2β regulates motility of cancer cells and suggest that LAP2β may have utility for diagnostics and therapeutics in digestive tract cancers

Nuclear envelope protein Lem2 is required for mouse development and regulates MAP and AKT kinases

The nuclear lamina, along with associated nuclear membrane proteins, is a nexus for regulating signaling in the nucleus. Numerous human diseases arise from mutations in lamina proteins, and experimental models for these disorders have revealed aberrant regulation of various signaling pathways. Previously, we reported that the inner nuclear membrane protein Lem2, which is expressed at high levels in muscle, promotes the differentiation of cultured myoblasts by attenuating ERK signaling. Here, we have analyzed mice harboring a disrupted allele for the Lem2 gene (Lemd2). No gross phenotypic defects were seen in heterozygotes, although muscle regeneration induced by cardiotoxin was delayed. By contrast, homozygous Lemd2 knockout mice died by E11.5. Although many normal morphogenetic hallmarks were observed in E10.5 knockout embryos, most tissues were substantially reduced in size. This was accompanied by activation of multiple MAP kinases (ERK1/2, JNK, p38) and AKT. Knockdown of Lem2 expression in C2C12 myoblasts also led to activation of MAP kinases and AKT. These findings indicate that Lemd2 plays an essential role in mouse embryonic development and that it is involved in regulating several signaling pathways. Since increased MAP kinase and AKT/mTORC signaling is found in other animal models for diseases linked to nuclear lamina proteins, LEMD2 should be considered to be another candidate gene for human disease

The Mutant Form of Lamin A that Causes Hutchinson-Gilford Progeria Is a Biomarker of Cellular Aging in Human Skin

Hutchinson-Gilford progeria syndrome (HGPS, OMIM 176670) is a rare disorder characterized by accelerated aging and early death, frequently from stroke or coronary artery disease. 90% of HGPS cases carry the LMNA G608G (GGC>GGT) mutation within exon 11 of LMNA, activating a splice donor site that results in production of a dominant negative form of lamin A protein, denoted progerin. Screening 150 skin biopsies from unaffected individuals (newborn to 97 years) showed that a similar splicing event occurs in vivo at a low level in the skin at all ages. While progerin mRNA remains low, the protein accumulates in the skin with age in a subset of dermal fibroblasts and in a few terminally differentiated keratinocytes. Progerin-positive fibroblasts localize near the basement membrane and in the papillary dermis of young adult skin; however, their numbers increase and their distribution reaches the deep reticular dermis in elderly skin. Our findings demonstrate that progerin expression is a biomarker of normal cellular aging and may potentially be linked to terminal differentiation and senescence in elderly individuals