プロテウス症候群の多面的な課題について
1National Human Genome Research Institute, Genetic Diseases Research Branch, National Institutes of Health, Bldg 49, Room 4A80, Bethesda, MD 20892-4472, USA. leslieb@helix.nih.gov
JAMA
|May 18, 2001
まとめ
プロテウス症候群は,複数の組織でモザイクの過剰成長を引き起こし,骨格の変形や腫瘍などの合併症を引き起こす. このレビューは,このまれな疾患の診断,自然史,および管理を網羅しています.
科学分野:
- 遺伝学と希少疾患について
- 発達生物学 発達生物学とは
- 臨床医学とは,臨床医学である.
背景:
- プロテウス症候群は,様々な組織のモザイク型過剰成長によって特徴づけられる希少で散発的な疾患です.
- 過剰成長は,皮膚,皮下組織,骨,中枢神経系,内臓に影響を与える可能性があります.
- 合併症には,骨格の変形,脂腫,腫瘍,および血栓塞栓症が含まれます.
研究 の 目的:
- プロテウス症候群の5歳の患者のケーススタディを紹介します.
- プロテウス症候群の診断,自然史,病因,および管理に関する現在の知識をレビューする.
主な方法:
- ケースレポートのプレゼンテーション.
- プロテウス症候群に関する文献レビュー.
主要な成果:
- 症例患者は,プロテウス症候群に関連した複数の合併症を示した.
- このレビューは,障害の多面的な側面に関する現在の理解をまとめています.
結論:
- プロテウス症候群は,その多様な医学的および心理的社会的な結果のために,患者のケアにおいて重要な課題を提示します.
- 総合的な理解と管理戦略は,被災者にとって極めて重要です.
関連する概念動画
The Proteasome
7.8K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
7.8K
Protein Import into the Peroxisomes
4.4K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
4.4K
Proteomics
7.5K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.5K
The Proteasome
1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K
The Proteasome Structure
2.2K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The proteasome is an...
2.2K
Overview of Protein Metabolism
4.5K
Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
4.5K


