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1.
Community Dent Health ; 29(1): 74-7, 2012 Mar.
Article in English | MEDLINE | ID: mdl-22482254

ABSTRACT

OBJECTIVE: The aim of the study was to determine the prevalence and awareness of particular types of oral parafunctions in young healthy students and any association with temporomandibular disorders (TMD). MATERIAL AND METHODS: The study was performed in a randomly selected group of 303 healthy students (mean age 18.8 years) from the vocational technical school in Wroclaw, Poland, who underwent a routine clinical examination and functional analysis of the mouth. On taking the history all subjects were asked about their awareness of various forms of parafunctional activity in their mouth. RESULTS: Almost all subjects revealed various oral parafunctions such as: bruxism, nail and pen biting, chewing gum, and biting the mucosa of lip or cheek. These habits were present singly or as double, triple or even fourfold coincidences in a single person. The most frequent oral parafunctions were habitual gum chewing and bruxism. Subjects were very seldom aware of the last parafunction. TMDs were more prevalent in the presence of bruxism than in other oral parafunctions. CONCLUSIONS: The studied students revealed various types of oral parafunctions, however most of them were not aware of clenching and grinding their teeth.


Subject(s)
Dental Occlusion, Traumatic/classification , Self Concept , Students/psychology , Adolescent , Awareness , Bites, Human/classification , Bites, Human/psychology , Bruxism/classification , Bruxism/psychology , Cheek/injuries , Chewing Gum , Dental Enamel/pathology , Dental Occlusion, Traumatic/psychology , Dentin/pathology , Humans , Lip/injuries , Male , Medical History Taking , Nail Biting/psychology , Self-Injurious Behavior/classification , Self-Injurious Behavior/psychology , Temporomandibular Joint Disorders/classification , Tooth Attrition/classification , Young Adult
2.
Article in English | MEDLINE | ID: mdl-14535056

ABSTRACT

The bacterial environment of the mouth cavity may be subjected to change under influence of various factors, such as surgical removal of neoplasm tumors and in consequence the wearing of post-surgical prostheses with obturators. The purpose of the paper was to study the conceivable differences in occurrence of particular types of microorganisms found on the margin of post-surgical cavities and on the prosthetic obturators. The performed microbiologic examinations revealed that more pathologic bacterial flora was found on the obturators than in the post-surgical cavities. The authors conclude that the post-surgical patients should pay more attention to the very accurate hygiene of their prostheses and the mouth cavity as well.


Subject(s)
Bacteria/classification , Maxilla/surgery , Palatal Obturators/microbiology , Adult , Aged , Aged, 80 and over , Bacillus/classification , Denture, Complete, Upper/microbiology , Epithelium/microbiology , Female , Humans , Male , Maxilla/microbiology , Maxillary Neoplasms/surgery , Middle Aged , Mouth Mucosa/microbiology , Pseudomonas/classification , Staphylococcus aureus/classification , Streptococcus/classification , Surgical Stomas/microbiology
3.
J Cell Sci ; 113 Pt 24: 4545-55, 2000 Dec.
Article in English | MEDLINE | ID: mdl-11082047

ABSTRACT

The Yck1p and Yck2p casein kinase 1 isoforms in yeast are essential peripheral plasma membrane-associated protein kinases with roles in endocytosis, cellular morphogenesis and cytokinesis. The membrane targeting of these cytoplasmically oriented protein kinases requires normal secretory pathway function, but specific targeting factors have not been identified. To learn more about Yckp targeting, we characterized mutations that cause synthetic lethality with impairment of Yck function. We report here that these include mutations in two gene products that function in protein trafficking. One of these is the previously described t-SNARE Tlg2p, which participates in recycling of proteins to the Golgi. The other is a previously uncharacterized protein, Rgp1p, which appears to have a similar function. Loss of either Tlg2p or Rgp1p causes inefficient localization of Yck2p, suggesting that its transport may be directed, in part, by a targeting factor that must be recycled back to the Golgi.


Subject(s)
Fungal Proteins/metabolism , Golgi Apparatus/metabolism , Guanine Nucleotide Exchange Factors , Membrane Proteins/metabolism , Membrane Transport Proteins , Proprotein Convertases , Protein Kinases/metabolism , Saccharomyces cerevisiae Proteins , Biomarkers , Carboxypeptidases/metabolism , Casein Kinases , Cathepsin A , Cell Membrane/metabolism , Fungal Proteins/genetics , Membrane Proteins/genetics , Qa-SNARE Proteins , R-SNARE Proteins , Saccharomyces cerevisiae , Subtilisins/metabolism , Vacuoles/metabolism
4.
Mol Biol Cell ; 10(4): 1077-92, 1999 Apr.
Article in English | MEDLINE | ID: mdl-10198058

ABSTRACT

Casein kinase 1 protein kinases are ubiquitous and abundant Ser/Thr-specific protein kinases with activity on acidic substrates. In yeast, the products of the redundant YCK1 and YCK2 genes are together essential for cell viability. Mutants deficient for these proteins display defects in cellular morphogenesis, cytokinesis, and endocytosis. Yck1p and Yck2p are peripheral plasma membrane proteins, and we report here that the localization of Yck2p within the membrane is dynamic through the cell cycle. Using a functional green fluorescent protein (GFP) fusion, we have observed that Yck2p is concentrated at sites of polarized growth during bud morphogenesis. At cytokinesis, GFP-Yck2p becomes associated with a ring at the bud neck and then appears as a patch of fluorescence, apparently coincident with the dividing membranes. The bud neck association of Yck2p at cytokinesis does not require an intact septin ring, and septin assembly is altered in a Yck-deficient mutant. The sites of GFP-Yck2p concentration and the defects observed for Yck-deficient cells together suggest that Yck plays distinct roles in morphogenesis and cytokinesis that are effected by differential localization.


Subject(s)
Casein Kinase I , Cell Cycle/physiology , Cytoskeletal Proteins/metabolism , Protein Kinases/metabolism , Saccharomyces cerevisiae Proteins , Saccharomyces cerevisiae/enzymology , Saccharomyces cerevisiae/growth & development , Casein Kinases , Cell Division , Cell Polarity , Cloning, Molecular , Diploidy , Green Fluorescent Proteins , Haploidy , Isoenzymes/biosynthesis , Isoenzymes/genetics , Isoenzymes/metabolism , Luminescent Proteins/biosynthesis , Morphogenesis , Mutagenesis , Open Reading Frames , Protein Kinases/biosynthesis , Protein Kinases/genetics , Recombinant Fusion Proteins/biosynthesis , Recombinant Fusion Proteins/metabolism , Saccharomyces cerevisiae/genetics
5.
Biol Reprod ; 59(3): 704-10, 1998 Sep.
Article in English | MEDLINE | ID: mdl-9716572

ABSTRACT

Transcriptional activation of the testis-specific histone H1t gene occurs in pachytene primary spermatocytes during spermatogenesis. Specific binding of testis nuclear proteins to a rat histone H1t promoter sequence, designated the H1t/TE element, correlates with the onset of transcription. This element, located between the H1t/AC box and the H1t/CCAAT box, contains inverted repeats of a shorter element. When the native rat H1t gene along with flanking sequences, including 2453 base pairs (bp) upstream and 3784 bp downstream from the coding region, was microinjected into mouse embryos, the offspring of the resulting transgenic mice transcribed the transgene in a tissue-specific manner and only in primary spermatocytes. In the present study the TE promoter element was deleted and replaced with a heterologous stuffer DNA fragment. When the mutant rat DNA fragment was used to create transgenic mice, offspring of the mice bearing the promoter mutation did not transcribe the rat H1t gene in any tissue. On the other hand, transcription of the rat H4t transgene, which is located approximately 1.5 kilobases downstream from the H1t gene, occurred in these animals. Therefore, these studies support the hypothesis that the TE element is essential for enhanced testis-specific transcription of the H1t gene in primary spermatocytes.


Subject(s)
Histones/genetics , Promoter Regions, Genetic , Spermatocytes/metabolism , Transcription, Genetic , Animals , Base Sequence , Gene Deletion , Humans , Male , Mice , Mice, Transgenic , Molecular Sequence Data , Mutagenesis , RNA, Messenger/metabolism , Rats , Repetitive Sequences, Nucleic Acid , TATA Box , Testis/metabolism
6.
EMBO J ; 16(14): 4194-204, 1997 Jul 16.
Article in English | MEDLINE | ID: mdl-9250663

ABSTRACT

In Saccharomyces cerevisiae, the redundant YCK1 and YCK2 genes (Yeast Casein Kinase 1) are required for viability. We describe here the molecular analysis of four mutations that eliminate the requirement for Yck activity. These mutations alter proteins that resemble the four subunits of clathrin adaptors (APs), with highest sequence similarity to those of the recently identified AP-3 complex. The four yeast subunits are associated in a high-molecular-weight complex. These proteins have no essential function and are not redundant for function with other yeast AP-related proteins. Combination of suppressor mutations with a clathrin heavy chain mutation (chc1-ts) confers no synthetic growth defects. However, a yck(ts) mutation shows a strong synthetic growth defect with chc1-ts. Moreover, endocytosis of Ste3p is dramatically decreased in yck(ts) cells and is partially restored by the AP suppressor mutations. These results suggest that vesicle trafficking at the plasma membrane requires the activity of Yck protein kinases, and that the new AP-related complex may participate in this process.


Subject(s)
Casein Kinase I , Monomeric Clathrin Assembly Proteins , Nerve Tissue Proteins/genetics , Phosphoproteins/genetics , Protein Kinases/genetics , Receptors, G-Protein-Coupled , Receptors, Pheromone , Saccharomyces cerevisiae Proteins , Saccharomyces cerevisiae/genetics , Suppression, Genetic/genetics , Adaptor Proteins, Vesicular Transport , Blotting, Western , Casein Kinases , Cell Division , Clathrin/genetics , Clathrin/metabolism , DNA Mutational Analysis , Endocytosis , Endosomes/metabolism , Membrane Proteins/metabolism , Molecular Sequence Data , Morphogenesis , Nerve Tissue Proteins/chemistry , Nerve Tissue Proteins/metabolism , Phosphoproteins/chemistry , Phosphoproteins/metabolism , Phosphorylation , Protein Conformation , Protein Kinases/metabolism , Receptors, Cell Surface/metabolism , Receptors, Mating Factor , Saccharomyces cerevisiae/enzymology , Saccharomyces cerevisiae/growth & development , Saccharomyces cerevisiae/metabolism
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