Relationship of Trimester-Specific Gestational Exposure to High Molecular Weight Phthalates with Neurodevelopment at 48 Months and Differences by Sex

2018 ◽  
Vol 2018 (1) ◽  
Author(s):  
Libni Avib Torres-Olascoaga ◽  
Marcela Tamayo y Ortiz ◽  
Lourdes Schnaas ◽  
Karen E Peterson ◽  
Martha María Téllez-Rojo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gestational Exposure ◽  
Relationship Of

scholarly journals Early Gestational Exposure to High-Molecular-Weight Phthalates and Its Association with 48-Month-Old Children’s Motor and Cognitive Scores

2020 ◽  
Vol 17 (21) ◽  
pp. 8150
Author(s):  
Libni A. Torres-Olascoaga ◽  
Deborah Watkins ◽  
Lourdes Schnaas ◽  
John D. Meeker ◽  
Maritsa Solano-Gonzalez ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Regression Models ◽  
First Trimester ◽  
Environmental Toxicants ◽  
Second Trimester ◽  
Linear Regression Models ◽  
Interaction Terms ◽  
Gestational Exposure ◽  
Early Life Exposure

In utero phthalate exposure has been associated with neurodevelopmental disorders, nevertheless, trimester-specific susceptibility remains understudied. Our aim was to identify susceptible windows to the effects of gestational High-Molecular-Weight Phthalates (HMWP) exposure on 48 months’ neurodevelopment. We measured six HMWP metabolites (MEHP, MEHHP, MEOHP, MECPP, MBzP and MCPP) in urine samples collected during each trimester from women in the Early Life Exposure in Mexico to Environmental Toxicants (ELEMENT) cohort (n = 218). We assessed children’s motor (MS), cognitive (GCI) and memory (MeS) abilities using McCarthy Scales of Children’s Abilities (MSCA). We used linear regression models to examine associations between trimester-specific phthalate metabolites and MSCA scores, adjusted for sex, gestational age, breastfeeding, and maternal IQ. Although phthalate concentrations were similar across trimesters, first and second trimester phthalates were inversely associated with MS and GCI, with first trimester associations with MS being the strongest and statistically significant. Stronger associations were seen with MS and GCI among boys compared to girls, however interaction terms were not statistically significant. Our results suggest that early gestation is a sensitive window of exposure to HMWP for neurodevelopment, particularly in boys. Regulations on phthalate content in food as well as pregnancy consumption guidelines are necessary to protect future generations.

scholarly journals Relationship of contact activation cofactor (CAC) procoagulant activity to kininogen

Blood ◽  
1977 ◽  
Vol 49 (6) ◽  
pp. 935-945 ◽  
Author(s):  
S Schiffman ◽  
P Lee ◽  
DI Feinstein ◽  
R Pecci
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Procoagulant Activity ◽  
Antigenic Determinants ◽  
High Molecular Weight Kininogen ◽  
Contact Activation ◽  
Precipitin Line ◽  
A Site ◽  
Relationship Of ◽  
The Relationship

Abstract Contact activation cofactor (CAC) facilitates the interaction of factors XI and XII. Patients lacking CAC have a coagulation defect and are deficient in high molecular weight kininogen. The coincidence of these two defects suggests that a single protein may be responsible for both physiologic functions. Immunologic and activity studies have been made on isolated CAC to clarify the relationship between CAC and kininogen. CAC forms a single precipitin line with anti-human kininogen, and antikininogen neutralizes CAC activity. CAC and high molecular weight kininogen show a reaction of identity on immunodiffusion against rabbit anti-CAC. Anti-CAC forms two precipitin lines with normal plasma which can be identified as high and low molecular weight kininogen. Monospecific immunoabsorbed anti-CAC forms a single precipitin line with plasma high molecular weight kininogen and neutralizes CAC activity. Cleavage of kinin fragment from CAC by insoluble trypsin or kalikrein does not proportionally reduce procoagulant activity. CAC neutralized by anti-CAC can release kinins on exposure to trypsin or kallikrein. The results support the conclusions that CAC procoagulant activity is a function of high molecular weight kininogen, that antigenic determinants unique to high molecular weight kininogen are shared by the CAC portion of the molecule, and that the clotting reactions may occur at a site removed from the kinin peptide.

scholarly journals The AMS Dating of Separate Fractions in Archaeology

Radiocarbon ◽  
1986 ◽  
Vol 28 (2A) ◽  
pp. 698-701 ◽  
Author(s):  
R J Batten ◽  
Richard Gillespie ◽  
J A J Gowlett ◽  
Rem Hedges
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Humic Acid ◽  
Carbon Source ◽  
High Molecular Weight ◽  
Complex Mixture ◽  
Small Samples ◽  
Radiocarbon Dates ◽  
Ams Dating ◽  
Relationship Of

The usefulness of radiocarbon dates in archaeology greatly depends on both the stratigraphic relationship of the sample submitted and on the origin and homogeneity of the measured carbon. For very small samples, stratigraphic relationships can raise additional problems of movement. In chemically well-characterized materials, the best example being collagen, the carbon source can be reasonably well purified. Many samples, however, survive as a complex mixture of high molecular weight polyphenolic materials, with properties between charcoals, humic acids, and lignins. Charred bone, eg, which rarely contains useful quantities of amino acids, and charred seeds, as well as ‘charcoal,’ frequently come into this category. For such samples, the likelihood of contamination by percolating soil humics is high. It is often possible to extract chemically different fractions and to compare the dates obtained. A less exact comparison can also be made for different samples from the same context. The results suggest that ‘humic’ acid dates can be reliable in a surprisingly frequent number of situations, and that where direct comparison is possible, the reliability can be individually assessed.

Influence Of High Molecular Weight Factor VIII On The Expression Of Factor VIII Procoagulant Activity

1981 ◽  
Author(s):  
W Muntean ◽  
W E Hathaway ◽  
R R Montgomery
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
High Molecular Weight ◽  
Procoagulant Activity ◽  
Two Stage ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
The One ◽  
Relationship Of ◽  
The Relationship

The relationship of the high molecular weight (HMW) moiety and low molecular weight (LMW) moiety of factor VIII in expressing procoagulant activity (VIII C) was studied. LMW VIII C was prepared by immunoadsorbent chromatography; HMW VIII was prepared by chromatographing hemophilic cryo- precipitate in 4% agarose. The LMW VIII C obtained by immunoadsorbent chromatography gave higher VIII C values when tested in the one stage partial thromboplastin time (PTT) system using von Willebrand’s disease plasma as substrate than using hemophilic plasma as substrate. This finding was shown to be due to the VIII related antigen (VIIIR:Ag) in the substrate plasmas. When the VIIIR:Ag was removed from the hemophilic substrate plasma by immuno-adsorption, the VIII C values obtained for the LMW VIII C were higher. Also, adding purified HMW VIII to the von Willebrand’s disease substrate plasma resulted in lower VIII C values for the LMW VIII C in the PTT system.When the LMW VIII C was tested in the two stage assay, all VIII C was adsorbed to A1(0H)3. The adsorption of the LMW VIII C was prevented by mixing it with hemophilic plasma. From normal undiluted plasma only 5-21% of VIII C and no VIII related antigen were adsorbed to A1(OH)3, but after activation of the factor VIII of normal plasma by small amounts of thrombin, most of the VIII C was adsorbed. No VIII related antigen was adsorbed after activation.Nevertheless, when unadsorbed LMW VIII C was assayed by the two stage method both with and without HMW VIII or VIIIR:Ag, the results were the same.Our studies suggest that VIIIR:Ag prevents to some extent the activation of LMW VIII C. LMW VIII C that is not bound or protected by VIIIRiAg is adsorbed from plasma by A1(0H)3. These findings may help explain the differences for VIII C found in some patients and certain clinical circumstances with the one and two stage assays.

scholarly journals Relationship of contact activation cofactor (CAC) procoagulant activity to kininogen

Blood ◽  
1977 ◽  
Vol 49 (6) ◽  
pp. 935-945
Author(s):  
S Schiffman ◽  
P Lee ◽  
DI Feinstein ◽  
R Pecci
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Procoagulant Activity ◽  
Antigenic Determinants ◽  
High Molecular Weight Kininogen ◽  
Contact Activation ◽  
Precipitin Line ◽  
A Site ◽  
Relationship Of ◽  
The Relationship

Contact activation cofactor (CAC) facilitates the interaction of factors XI and XII. Patients lacking CAC have a coagulation defect and are deficient in high molecular weight kininogen. The coincidence of these two defects suggests that a single protein may be responsible for both physiologic functions. Immunologic and activity studies have been made on isolated CAC to clarify the relationship between CAC and kininogen. CAC forms a single precipitin line with anti-human kininogen, and antikininogen neutralizes CAC activity. CAC and high molecular weight kininogen show a reaction of identity on immunodiffusion against rabbit anti-CAC. Anti-CAC forms two precipitin lines with normal plasma which can be identified as high and low molecular weight kininogen. Monospecific immunoabsorbed anti-CAC forms a single precipitin line with plasma high molecular weight kininogen and neutralizes CAC activity. Cleavage of kinin fragment from CAC by insoluble trypsin or kalikrein does not proportionally reduce procoagulant activity. CAC neutralized by anti-CAC can release kinins on exposure to trypsin or kallikrein. The results support the conclusions that CAC procoagulant activity is a function of high molecular weight kininogen, that antigenic determinants unique to high molecular weight kininogen are shared by the CAC portion of the molecule, and that the clotting reactions may occur at a site removed from the kinin peptide.

Microtubule motors and other maps

1990 ◽  
Vol 48 (3) ◽  
pp. 1-1
Author(s):  
Richard B. Vallee
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Structural Components ◽  
Microtubule Associated Proteins ◽  
Microtubule Motors ◽  
Associated Proteins ◽  
The Subject ◽  
Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

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