Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation

Hart, Thomas C.; Hart, Patricia; Michalec, Michael; Zhang, Y; Marazita, Mary L.; Cooper, Margaret E.; Yassin, Othman M.; Nusier, Mohamad; Walker, Stephen J.

doi:10.1136/jmg.37.2.95

Cited by 98 publications

(97 citation statements)

References 35 publications

(28 reference statements)

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“…34 Interestingly, cathepsin C gene mutations were also identified in familial prepubertal periodontitis. 35 Another related syndrome, Haim-Munk syndrome, was also found to have a mutation in the same gene and is now considered to be an allelic variant of PLS. 36 …”

Section: Discussionmentioning

confidence: 99%

Pyogenic Liver Abscess and Papillon-Lefèvre Syndrome: Not a Rare Association

Almuneef¹,

Khenaizan

Ajaji³

et al. 2003

Pediatrics

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ABSTRACT. Papillon-Lefèvre syndrome is a rare, autosomal recessive disease comprising palmoplantar keratoderma and periodontitis. Pyogenic liver abscess is an increasingly recognized complication. We report a new case of this association and review the current literature. Pediatrics 2003;111:e85-e88. URL: http://www.pediatrics. org/cgi/content/full/111/1/e85; Papillon-Lefèvre syndrome, liver abscess.

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Section: Discussionmentioning

confidence: 99%

Pyogenic Liver Abscess and Papillon-Lefèvre Syndrome: Not a Rare Association

Almuneef¹,

Khenaizan

Ajaji³

et al. 2003

Pediatrics

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“…PapillonLefèvre syndrome is usually first diagnosed by dentists. Both syndromes have now been shown to result from mutations in the DPP I gene (Hart et al, 1999(Hart et al, , 2000Toomes et al, 1999). Why loss of this widely distributed lysosomal enzyme should preferentially affect these tissues is unknown, although ChediakHigashi syndrome, which also affects lysosomes, is also associated with immune dysfunction and severe early-onset periodontal disease (Tempel et al, 1972;Introne et al, 1999).…”

Section: (Ii) Functions Of Dpp I and Its Role In Pre-pubertal Periodomentioning

confidence: 99%

“…Missense mutations in the DPP I gene, located at 11q14, have very recently been shown to be responsible for one recessive form of pre-pubertal periodontitis, a rapidly progressing, heritable form of the disease that affects the primary dentition (Hart et al, 2000). Two distinct autosomal-recessive palmoplantar keratoderma disorders, Papillon-Lefèvre syndrome and Haim-Munk syndrome, characterized by hyperkeratosis of specific epithelial areas, particularly the hands and feet, are also characterized by severe early-onset periodontitis, resulting in the loss of the primary and secondary dentition.…”

Section: (Ii) Functions Of Dpp I and Its Role In Pre-pubertal Periodomentioning

confidence: 99%

Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

158

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Cysteine peptidases (CPs) are phylogenetically ubiquitous enzymes that can be classified into clans of evolutionarily independent proteins based on the structural organization of the active site. In mammals, two of the major clans represented in the genome are: the CA clan, whose members share a structure and evolutionary history with papain; and the CD clan, which includes the legumains and caspases. This review focuses on the properties of these enzymes, with an emphasis on their potential roles in the oral cavity. The human genome encodes at least (but possibly no more than) 11 distinct enzymes, called cathepsins, that are members of the papain family C1A. Ten of these are present in rodents, which also carry additional genes encoding other cathepsins and cathepsin-like proteins. Human cathepsins are best known from the ubiquitously expressed lysosomal cathepsins B, H, and L, and dipeptidyl peptidase I (DPP I), which until recently were considered to mediate primarily "housekeeping" functions in the cell. However, mutations in DPP I have now been shown to underlie Papillon-Lefèvre syndrome and pre-pubertal periodontitis. Other cathepsins are involved in tissue-specific functions such as bone remodeling, but relatively little is known about the functions of several recently discovered enzymes. Collectively, CPs participate in multiple host systems that are active in health and in disease. They are involved in tissue remodeling and turnover of the extracellular matrix, immune system function, and modulation and alteration of cell function. Intracellularly, CPs function in diverse processes including normal protein turnover, antigen and proprotein processing, and apoptosis. Extracellularly, they can contribute directly to the degradation of foreign proteins and the extracellular matrix. However, CPs can also participate in proteolytic cascades that amplify the degradative capacity, potentially leading to pathological damage, and facilitating the penetration of tissues by cancer cells. We know relatively little regarding the role of human CPs in the oral cavity in health or disease. Most studies to date have focused on the potential use of the lysosomal enzymes as markers for periodontal disease activity. Human saliva contains high levels of cystatins, which are potent CP inhibitors. Although these proteins are presumed to serve a protective function, their in vivo targets are unknown, and it remains to be discovered whether they serve to control any human CP activity.

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“…An IL1B allele has been reported to be in linkage disequilibrium with generalized aggressive periodontitis. 31 …”

Section:  Early Onset Periodontits (Aggressive Periodontitis)mentioning

confidence: 99%