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  1. Article ; Online: Alterations of elastin in female reproductive tissues arising from advancing parity.

    Dhital, Basant / Downing, Keith T / Gul-E-Noor, Farhana / Landau, Yakov / Rathod, Pratikkumar / Hirsch, Shari / Chang, Emmanuel J / Boutis, Gregory S

    Archives of biochemistry and biophysics

    2019  Volume 666, Page(s) 127–137

    Abstract: Female reproductive tissues undergo significant alterations during pregnancy, which may compromise the structural integrity of extracellular matrix proteins. Here, we report on modifications of elastic fibers, which are primarily composed of elastin and ... ...

    Abstract Female reproductive tissues undergo significant alterations during pregnancy, which may compromise the structural integrity of extracellular matrix proteins. Here, we report on modifications of elastic fibers, which are primarily composed of elastin and believed to provide a scaffold to the reproductive tissues, due to parity and parturition. Elastic fibers from the upper vaginal wall of virgin Sprague Dawley rats were investigated and compared to rats having undergone one, three, or more than five pregnancies. Optical microscopy was used to study fiber level changes. Mass spectrometry,
    MeSH term(s) Animals ; Desmosine/metabolism ; Elastic Tissue/chemistry ; Elastic Tissue/metabolism ; Elastin/chemistry ; Elastin/metabolism ; Female ; Matrix Metalloproteinase 2/metabolism ; Matrix Metalloproteinase 9/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Parity/physiology ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Pregnancy ; Protein Structure, Secondary ; Rats ; Rats, Sprague-Dawley ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Tissue Inhibitor of Metalloproteinase-1/metabolism ; Vagina/metabolism
    Chemical Substances Peptide Fragments ; TIMP1 protein, rat ; Tissue Inhibitor of Metalloproteinase-1 ; Desmosine (11003-57-9) ; Elastin (9007-58-3) ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; Mmp2 protein, rat (EC 3.4.24.24) ; Matrix Metalloproteinase 9 (EC 3.4.24.35) ; Mmp9 protein, rat (EC 3.4.24.35)
    Language English
    Publishing date 2019-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2019.03.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Alterations of elastin in female reproductive tissues arising from advancing parity

    Dhital, Basant / Downing, Keith T / Gul-E-Noor, Farhana / Landau, Yakov / Rathod, Pratikkumar / Hirsch, Shari / Chang, Emmanuel J / Boutis, Gregory S

    Archives of biochemistry and biophysics. 2019 May 15, v. 666

    2019  

    Abstract: Female reproductive tissues undergo significant alterations during pregnancy, which may compromise the structural integrity of extracellular matrix proteins. Here, we report on modifications of elastic fibers, which are primarily composed of elastin and ... ...

    Abstract Female reproductive tissues undergo significant alterations during pregnancy, which may compromise the structural integrity of extracellular matrix proteins. Here, we report on modifications of elastic fibers, which are primarily composed of elastin and believed to provide a scaffold to the reproductive tissues, due to parity and parturition. Elastic fibers from the upper vaginal wall of virgin Sprague Dawley rats were investigated and compared to rats having undergone one, three, or more than five pregnancies. Optical microscopy was used to study fiber level changes. Mass spectrometry, 13C and 2H NMR, was applied to study alterations of elastin from the uterine horns. Spectrophotometry was used to measure matrix metalloproteinases-2,9 and tissue inhibitor of metalloproteinase-1 concentration changes in the uterine horns. Elastic fibers were found to exhibit increase in tortuosity and fragmentation with increased pregnancies. Surprisingly, secondary structure, dynamics, and crosslinking of elastin from multiparous cohorts appear similar to healthy mammalian tissues, despite fragmentation observed at the fiber level. In contrast, elastic fibers from virgin and single pregnancy cohorts are less fragmented and comprised of elastin exhibiting structure and dynamics distinguishable from multiparous groups, with reduced crosslinking. These alterations were correlated to matrix metalloproteinases-2,9 and tissue inhibitor of metalloproteinase-1 concentrations. This work indicates that fiber level alterations resulting from pregnancy and/or parturition, such as fragmentation, rather than secondary structure (e.g. elastin crosslinking density), appear to govern scaffolding characteristics in the female reproductive tissues.
    Keywords carbon ; crosslinking ; elastin ; females ; laboratory animals ; light microscopy ; mass spectrometry ; nuclear magnetic resonance spectroscopy ; parturition ; pregnancy ; rats ; stable isotopes ; tissues ; uterus
    Language English
    Dates of publication 2019-0515
    Size p. 127-137.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2019.03.008
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Pregnancy-Induced Dynamical and Structural Changes of Reproductive Tract Collagen.

    Dhital, Basant / Gul-E-Noor, Farhana / Downing, Keith T / Hirsch, Shari / Boutis, Gregory S

    Biophysical journal

    2016  Volume 111, Issue 1, Page(s) 57–68

    Abstract: The tissues and organs of the female reproductive tract and pelvic floor undergo significant remodeling and alterations to allow for fetal growth and birth. In this work, we report on a study of the alterations of murine reproductive tract collagen ... ...

    Abstract The tissues and organs of the female reproductive tract and pelvic floor undergo significant remodeling and alterations to allow for fetal growth and birth. In this work, we report on a study of the alterations of murine reproductive tract collagen resulting from pregnancy and parturition by spectrophotometry, histology, and (13)C, (2)H nuclear magnetic resonance (NMR). Four different cohorts of rats were investigated that included virgin, multiparous, two- and fourteen-day postpartum primiparous rats. (13)C CPMAS NMR revealed small chemical shift differences across the cohorts. The measured H-C internuclear correlation times indicated differences in dynamics of some motifs. However, the dynamics of the major amino acids, e.g., Gly, remained unaltered with respect to parity. (2)H NMR relaxation measurements revealed an additional water reservoir in the postpartum and multiparous cohorts pointing to redistribution of water due to pregnancy and/or parturition. Spectrophotometric measurements indicated that the collagen content in virgin rats was highest. Histological analysis of the upper vaginal wall indicated a signature of collagen fiber dissociation with smooth muscle and a change in the density of collagen fibers in multiparous rats.
    MeSH term(s) Animals ; Collagen/chemistry ; Collagen/metabolism ; Female ; Parity ; Postpartum Period ; Pregnancy ; Rats ; Rats, Sprague-Dawley ; Vagina/metabolism ; Water/metabolism
    Chemical Substances Water (059QF0KO0R) ; Collagen (9007-34-5)
    Language English
    Publishing date 2016-07-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2016.05.049
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Quantification of desmosine and isodesmosine using MALDI-ion trap tandem mass spectrometry.

    Rathod, Pratikkumar / Kaur, Manjeet / Ho, Hsin-Pin / Louis, Marissa E / Dhital, Basant / Durlik, Philip / Boutis, Gregory S / Mark, Kevin J / Lee, Jong I / Chang, Emmanuel J

    Analytical and bioanalytical chemistry

    2018  Volume 410, Issue 26, Page(s) 6881–6889

    Abstract: Desmosine (Des) and isodesmosine (Isodes), cross-linking amino acids in the biomolecule elastin, may be used as biomarkers for various pathological conditions associated with elastin degradation. The current study presents a novel approach to quantify ... ...

    Abstract Desmosine (Des) and isodesmosine (Isodes), cross-linking amino acids in the biomolecule elastin, may be used as biomarkers for various pathological conditions associated with elastin degradation. The current study presents a novel approach to quantify Des and Isodes using matrix-assisted laser desorption ionization (MALDI)-tandem mass spectrometry (MS
    MeSH term(s) Desmosine/analysis ; Desmosine/blood ; Desmosine/chemistry ; Desmosine/urine ; Humans ; Limit of Detection ; Reference Standards ; Reproducibility of Results ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Tandem Mass Spectrometry/methods
    Chemical Substances Desmosine (11003-57-9)
    Language English
    Publishing date 2018-07-31
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 201093-8
    ISSN 1618-2650 ; 0016-1152 ; 0372-7920
    ISSN (online) 1618-2650
    ISSN 0016-1152 ; 0372-7920
    DOI 10.1007/s00216-018-1288-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Ultraviolet radiation reduces desmosine cross-links in elastin.

    Dhital, Basant / Durlik, Philip / Rathod, Pratikkumar / Gul-E-Noor, Farhana / Wang, Zhixiao / Sun, Cheng / Chang, Emmanuel J / Itin, Boris / Boutis, Gregory S

    Biochemistry and biophysics reports

    2017  Volume 10, Page(s) 172–177

    Abstract: Elastic fibers, a major component of the extracellular matrix of the skin, are often exposed to ultraviolet (UV) radiation throughout mammalian life. We report on ... ...

    Abstract Elastic fibers, a major component of the extracellular matrix of the skin, are often exposed to ultraviolet (UV) radiation throughout mammalian life. We report on an
    Language English
    Publishing date 2017-04-06
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2831046-9
    ISSN 2405-5808
    ISSN 2405-5808
    DOI 10.1016/j.bbrep.2017.04.002
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  6. Article: Quantification of desmosine and isodesmosine using MALDI-ion trap tandem mass spectrometry

    Rathod, Pratikkumar / Kaur, Manjeet / Ho, Hsin-Pin / Louis, Marissa E / Dhital, Basant / Durlik, Philip / Boutis, Gregory S / Mark, Kevin J / Lee, Jong I / Chang, Emmanuel J

    Analytical and bioanalytical chemistry. 2018 Oct., v. 410, no. 26

    2018  

    Abstract: Desmosine (Des) and isodesmosine (Isodes), cross-linking amino acids in the biomolecule elastin, may be used as biomarkers for various pathological conditions associated with elastin degradation. The current study presents a novel approach to quantify ... ...

    Abstract Desmosine (Des) and isodesmosine (Isodes), cross-linking amino acids in the biomolecule elastin, may be used as biomarkers for various pathological conditions associated with elastin degradation. The current study presents a novel approach to quantify Des and Isodes using matrix-assisted laser desorption ionization (MALDI)-tandem mass spectrometry (MS2) in a linear ion trap coupled to a vacuum MALDI source. MALDI-MS2 analyses of Des and Isodes are performed using stable-isotope-labeled desmosine d4 (labeled-Des) as an internal standard in different biological fluids, such as urine and serum. The method demonstrated linearity over two orders of magnitude with a detection limit of 0.02 ng/μL in both urine and serum without enrichment prior to mass spectrometry, and relative standard deviation of < 5%. The method is used to evaluate the time-dependent degradation of Des upon UV irradiation (254 nm) and found to be consistent with quantification by 1H NMR. This is the first characterized MALDI-MS2 method for quantification of Des and Isodes and illustrates the potential of MALDI-ion trap MS2 for effective quantification of biomolecules. The reported method represents improvement over current liquid chromatography-based methods with respect to analysis time and solvent consumption, while maintaining similar analytical characteristics. Graphical abstract ᅟ
    Keywords amino acids ; biomarkers ; blood serum ; crosslinking ; desorption ; elastin ; ionization ; liquid chromatography ; nuclear magnetic resonance spectroscopy ; solvents ; statistical analysis ; tandem mass spectrometry ; ultraviolet radiation ; urine
    Language English
    Dates of publication 2018-10
    Size p. 6881-6889.
    Publishing place Springer Berlin Heidelberg
    Document type Article
    ISSN 1618-2642
    DOI 10.1007/s00216-018-1288-z
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  7. Article ; Online: Ultraviolet radiation reduces desmosine cross-links in elastin

    Basant Dhital / Philip Durlik / Pratikkumar Rathod / Farhana Gul-E-Noor / Zhixiao Wang / Cheng Sun / Emmanuel J. Chang / Boris Itin / Gregory S. Boutis

    Biochemistry and Biophysics Reports, Vol 10, Iss C, Pp 172-

    2017  Volume 177

    Abstract: Elastic fibers, a major component of the extracellular matrix of the skin, are often exposed to ultraviolet (UV) radiation throughout mammalian life. We report on an in vitro study of the alterations in bovine nuchal ligament elastic fibers resulting ... ...

    Abstract Elastic fibers, a major component of the extracellular matrix of the skin, are often exposed to ultraviolet (UV) radiation throughout mammalian life. We report on an in vitro study of the alterations in bovine nuchal ligament elastic fibers resulting from continuous UV-A exposure by the use of transmission electron microscopy (TEM), histology, mass spectrometry, and solid state 13C NMR methodologies. TEM images reveal distinct cracks in elastic fibers as a result of UV-A irradiation and histological measurements show a disruption in the regular array of elastic fibers present in unirradiated samples; elastic fibers appear shorter, highly fragmented, and thinner after UV-A treatment. Magic angle spinning 13C NMR was applied to investigate possible secondary structural changes or dynamics in the irradiated samples; our spectra reveal no differences between UV-A irradiated and non-irradiated samples. Lastly, MALDI mass spectrometry indicates that the concentration of desmosine, which forms cross-links in elastin, is observed to decrease by 11 % following 9 days of continuous UV-A irradiation, in comparison to unirradiated samples. These alterations presumably play a significant role in the loss of elasticity observed in UV exposed skin.
    Keywords Elastin ; Elastic fiber ; Ultraviolet radiation ; Nuclear magnetic resonance ; MALDI ; Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
    Language English
    Publishing date 2017-07-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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